3WT4 | pdb_00003wt4

Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Peptidase_M18_2nd	e3wt4A2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: Peptidase_M18_2nd	ECOD (1.6)
A	Peptidase_M18_1st	e3wt4A1	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: Peptidase_M18_1st	ECOD (1.6)
B	Peptidase_M18_2nd	e3wt4B2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: Peptidase_M18_2nd	ECOD (1.6)
B	Peptidase_M18_1st	e3wt4B1	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: Peptidase_M18_1st	ECOD (1.6)
C	Peptidase_M18_2nd	e3wt4C2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: Peptidase_M18_2nd	ECOD (1.6)
C	Peptidase_M18_1st	e3wt4C1	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: Peptidase_M18_1st	ECOD (1.6)
D	Peptidase_M18_2nd	e3wt4D2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: Peptidase_M18_2nd	ECOD (1.6)
D	Peptidase_M18_1st	e3wt4D1	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: Peptidase_M18_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
A	2.30.250.10	Mainly Beta	Roll	Aminopeptidase i, Domain 2	Aminopeptidase i, Domain 2	CATH (4.3.0)
B	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
B	2.30.250.10	Mainly Beta	Roll	Aminopeptidase i, Domain 2	Aminopeptidase i, Domain 2	CATH (4.3.0)
C	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
C	2.30.250.10	Mainly Beta	Roll	Aminopeptidase i, Domain 2	Aminopeptidase i, Domain 2	CATH (4.3.0)
D	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
D	2.30.250.10	Mainly Beta	Roll	Aminopeptidase i, Domain 2	Aminopeptidase i, Domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF02127	Aminopeptidase I zinc metalloprotease (M18) (Peptidase_M18)	Aminopeptidase I zinc metalloprotease (M18)	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Probable M18 family aminopeptidase 2	peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity catalytic activity cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding aminopeptidase activity exopeptidase activity	proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR022984	M18 family aminopeptidase 2, putative	Family
A, B, C, D	IPR023358	Peptidase M18, domain 2	Homologous Superfamily
A, B, C, D	IPR001948	Peptidase M18	Family

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.