1MT5

CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: OPM
Membrane Protein Annotation: mpstruc
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1mt5a_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Fatty acid amide hydrolase (oleamide hydrolase)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
B	d1mt5b_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Fatty acid amide hydrolase (oleamide hydrolase)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
C	d1mt5c_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Fatty acid amide hydrolase (oleamide hydrolase)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
D	d1mt5d_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Fatty acid amide hydrolase (oleamide hydrolase)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
E	d1mt5e_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Fatty acid amide hydrolase (oleamide hydrolase)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
F	d1mt5f_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Fatty acid amide hydrolase (oleamide hydrolase)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
G	d1mt5g_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Fatty acid amide hydrolase (oleamide hydrolase)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
H	d1mt5h_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Fatty acid amide hydrolase (oleamide hydrolase)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
I	d1mt5i_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Fatty acid amide hydrolase (oleamide hydrolase)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
J	d1mt5j_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Fatty acid amide hydrolase (oleamide hydrolase)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
K	d1mt5k_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Fatty acid amide hydrolase (oleamide hydrolase)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
L	d1mt5l_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Fatty acid amide hydrolase (oleamide hydrolase)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
M	d1mt5m_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Fatty acid amide hydrolase (oleamide hydrolase)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
N	d1mt5n_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Fatty acid amide hydrolase (oleamide hydrolase)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
O	d1mt5o_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Fatty acid amide hydrolase (oleamide hydrolase)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
P	d1mt5p_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Fatty acid amide hydrolase (oleamide hydrolase)	Norway rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Amidase signature (AS) enzymes	8031386	4002446	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Amidase signature (AS) enzymes	8043764	3001251	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Amidase signature (AS) enzymes	8043764	3001251	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Amidase signature (AS) enzymes	8043764	3001251	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Amidase signature (AS) enzymes	8043764	3001251	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Amidase signature (AS) enzymes	8043764	3001251	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Amidase signature (AS) enzymes	8043764	3001251	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Amidase signature (AS) enzymes	8043764	3001251	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Amidase signature (AS) enzymes	8043764	3001251	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	Amidase signature (AS) enzymes	8043764	3001251	SCOP2B (2022-06-29)
J	SCOP2B Superfamily	Amidase signature (AS) enzymes	8043764	3001251	SCOP2B (2022-06-29)
K	SCOP2B Superfamily	Amidase signature (AS) enzymes	8043764	3001251	SCOP2B (2022-06-29)
L	SCOP2B Superfamily	Amidase signature (AS) enzymes	8043764	3001251	SCOP2B (2022-06-29)
M	SCOP2B Superfamily	Amidase signature (AS) enzymes	8043764	3001251	SCOP2B (2022-06-29)
N	SCOP2B Superfamily	Amidase signature (AS) enzymes	8043764	3001251	SCOP2B (2022-06-29)
O	SCOP2B Superfamily	Amidase signature (AS) enzymes	8043764	3001251	SCOP2B (2022-06-29)
P	SCOP2B Superfamily	Amidase signature (AS) enzymes	8043764	3001251	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Amidase	e1mt5A1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
B	Amidase	e1mt5B1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
C	Amidase	e1mt5C1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
D	Amidase	e1mt5D1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
E	Amidase	e1mt5E1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
F	Amidase	e1mt5F1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
G	Amidase	e1mt5G1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
H	Amidase	e1mt5H1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
I	Amidase	e1mt5I1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
J	Amidase	e1mt5J1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
K	Amidase	e1mt5K1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
L	Amidase	e1mt5L1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
M	Amidase	e1mt5M1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
N	Amidase	e1mt5N1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
O	Amidase	e1mt5O1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
P	Amidase	e1mt5P1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
B	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
C	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
D	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
E	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
F	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
G	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
H	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
I	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
J	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
K	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
L	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
M	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
N	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
O	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
P	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	PF01425	Amidase (Amidase)	Amidase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	Fatty-acid amide hydrolase	amidase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds binding lipid binding hydrolase activity, acting on ester bonds carboxylic ester hydrolase activity monoacylglycerol lipase activity lipase activity fatty acid amide hydrolase activity phospholipid binding identical protein binding amidase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds binding lipid binding hydrolase activity, acting on ester bonds carboxylic ester hydrolase activity monoacylglycerol lipase activity lipase activity fatty acid amide hydrolase activity phospholipid binding identical protein binding protein binding	fatty acid metabolic process oxoacid metabolic process carboxylic acid metabolic process primary metabolic process metabolic process cellular process small molecule metabolic process monocarboxylic acid metabolic process organic acid metabolic process lipid metabolic process regulation of tube diameter multicellular organismal process regulation of biological process system process fatty acid metabolic process oxoacid metabolic process carboxylic acid metabolic process primary metabolic process metabolic process cellular process small molecule metabolic process monocarboxylic acid metabolic process organic acid metabolic process lipid metabolic process regulation of tube diameter multicellular organismal process regulation of biological process system process regulation of tube size regulation of system process biological regulation positive regulation of biological process positive regulation of vasoconstriction circulatory system process regulation of blood circulation vascular process in circulatory system regulation of vasoconstriction positive regulation of multicellular organismal process regulation of multicellular organismal process blood vessel diameter maintenance regulation of biological quality vasoconstriction blood circulation regulation of anatomical structure size lipid catabolic process catabolic process organic acid catabolic process fatty acid catabolic process cellular catabolic process monocarboxylic acid catabolic process carboxylic acid catabolic process small molecule catabolic process trans-synaptic signaling regulation of signaling regulation of cellular process signaling trans-synaptic signaling, modulating synaptic transmission modulation of chemical synaptic transmission trans-synaptic signaling by endocannabinoid cell-cell signaling cell communication chemical synaptic transmission synaptic signaling regulation of trans-synaptic signaling by endocannabinoid, modulating synaptic transmission regulation of trans-synaptic signaling trans-synaptic signaling by lipid, modulating synaptic transmission anterograde trans-synaptic signaling trans-synaptic signaling by lipid regulation of cell communication trans-synaptic signaling by endocannabinoid, modulating synaptic transmission neutral lipid metabolic process monoacylglycerol catabolic process neutral lipid catabolic process glycerolipid catabolic process acylglycerol catabolic process monoacylglycerol metabolic process glycerolipid metabolic process acylglycerol metabolic process	membrane-bounded organelle cellular anatomical structure organelle membrane organelle membrane Golgi membrane intracellular anatomical structure Golgi apparatus intracellular membrane-bounded organelle endomembrane system intracellular organelle bounding membrane of organelle cytoplasm presynapse membrane-bounded organelle cellular anatomical structure organelle membrane organelle membrane Golgi membrane intracellular anatomical structure Golgi apparatus intracellular membrane-bounded organelle endomembrane system intracellular organelle bounding membrane of organelle cytoplasm presynapse synapse cell junction postsynapse glutamatergic synapse organelle subcompartment endoplasmic reticulum subcompartment nuclear outer membrane-endoplasmic reticulum membrane network endoplasmic reticulum endoplasmic reticulum membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	IPR036928	Amidase signature (AS) superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	IPR052096	Endocannabinoid-regulating amidase	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	IPR023631	Amidase signature domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	IPR020556	Amidase, conserved site	Conserved Site

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	OPM				Amidase signature (AS) enzymes

Membrane Protein Annotation: mpstruc mpstruc Database Homepage

Chains	Resource Link	Group	Subgroup	Protein
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	mpstruc	MONOTOPIC MEMBRANE PROTEINS	Hydrolases	Fatty acid amide hydrolase

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	fatty acid amide hydrolase M-CSA #731	Mammalian fatty acid amide hydrolase (FAAH) degrades fatty acid primary amides and ethanolamides such as anandamide and oleamide. Anandamide binds and activates cannabinoid and vanilloid receptors exerting an analgesic and cannabinoid effects while oleamide has been found to be sleep inducing. Rat FAAH is an integral membrane protein. The wild type protein hydrolyses esters and amides at the same rate but the Lys142Ala mutant hydrolyses esters more rapidly than amides.	Defined by 7 residues: LYS:A-106 [auth A-142]SER:A-181 [auth A-217]SER:A-182 [auth A-218]ILE:A-202 [auth A-238]GLY:A-203 [auth A-239]GLY:A-204 [auth A-240]SER:A-205 [auth A-241] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.1 (PDB Primary Data) Search M-CSA Motif + EC 3.1 EC: 3.1.1 (UniProt) Search M-CSA Motif + EC 3.1.1 EC: 3.5.1.99 (UniProt) Search M-CSA Motif + EC 3.5.1.99

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.