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Crystal structure of MccF-like protein (BA_5613) in the complex with aspartyl sulfamoyl adenylate

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)
B	Peptidase_S66_N	e5usdB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Class I glutamine amidotransferase-like	F: Peptidase_S66_N	ECOD (1.6)
B	Peptidase_S66_C	e5usdB2	A: a/b three-layered sandwiches	X: The swivelling beta/beta/alpha domains	H: The swivelling beta/beta/alpha domain (From Topology)	T: The swivelling beta/beta/alpha domain	F: Peptidase_S66_C	ECOD (1.6)
C	Peptidase_S66_N	e5usdC2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Class I glutamine amidotransferase-like	F: Peptidase_S66_N	ECOD (1.6)
C	Peptidase_S66_C	e5usdC1	A: a/b three-layered sandwiches	X: The swivelling beta/beta/alpha domains	H: The swivelling beta/beta/alpha domain (From Topology)	T: The swivelling beta/beta/alpha domain	F: Peptidase_S66_C	ECOD (1.6)
D	Peptidase_S66_N	e5usdD2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Class I glutamine amidotransferase-like	F: Peptidase_S66_N	ECOD (1.6)
D	Peptidase_S66_C	e5usdD1	A: a/b three-layered sandwiches	X: The swivelling beta/beta/alpha domains	H: The swivelling beta/beta/alpha domain (From Topology)	T: The swivelling beta/beta/alpha domain	F: Peptidase_S66_C	ECOD (1.6)
A	Peptidase_S66_N	e5usdA1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Class I glutamine amidotransferase-like	F: Peptidase_S66_N	ECOD (1.6)
A	Peptidase_S66_C	e5usdA2	A: a/b three-layered sandwiches	X: The swivelling beta/beta/alpha domains	H: The swivelling beta/beta/alpha domain (From Topology)	T: The swivelling beta/beta/alpha domain	F: Peptidase_S66_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.50.10740	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Murein tetrapeptidase LD-carboxypeptidase, N-terminal domain	CATH (4.3.0)
B	3.50.30.60	Alpha Beta	3-Layer(bba) Sandwich	Glucose Oxidase	domain 1	CATH (4.3.0)
C	3.40.50.10740	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Murein tetrapeptidase LD-carboxypeptidase, N-terminal domain	CATH (4.3.0)
C	3.50.30.60	Alpha Beta	3-Layer(bba) Sandwich	Glucose Oxidase	domain 1	CATH (4.3.0)
D	3.40.50.10740	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Murein tetrapeptidase LD-carboxypeptidase, N-terminal domain	CATH (4.3.0)
D	3.50.30.60	Alpha Beta	3-Layer(bba) Sandwich	Glucose Oxidase	domain 1	CATH (4.3.0)
A	3.40.50.10740	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Murein tetrapeptidase LD-carboxypeptidase, N-terminal domain	CATH (4.3.0)
A	3.50.30.60	Alpha Beta	3-Layer(bba) Sandwich	Glucose Oxidase	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF17676	LD-carboxypeptidase C-terminal domain (Peptidase_S66C)	LD-carboxypeptidase C-terminal domain	Muramoyl-tetrapeptide carboxypeptidase hydrolyses a peptide bond between a di-basic amino acid and the C-terminal D-alanine in the tetrapeptide moiety in peptidoglycan. This cleaves the bond between an L- and a D-amino acid. ...	Muramoyl-tetrapeptide carboxypeptidase hydrolyses a peptide bond between a di-basic amino acid and the C-terminal D-alanine in the tetrapeptide moiety in peptidoglycan. This cleaves the bond between an L- and a D-amino acid. The function of this activity is in murein recycling. This family also includes the microcin c7 self-immunity protein Swiss:Q47511. This family corresponds to Merops family S66.	Domain
A, B, C, D	PF02016	LD-carboxypeptidase N-terminal domain (Peptidase_S66)	LD-carboxypeptidase N-terminal domain	Muramoyl-tetrapeptide carboxypeptidase hydrolyses a peptide bond between a di-basic amino acid and the C-terminal D-alanine in the tetrapeptide moiety in peptidoglycan. This cleaves the bond between an L- and a D-amino acid. The function of this acti ...	Muramoyl-tetrapeptide carboxypeptidase hydrolyses a peptide bond between a di-basic amino acid and the C-terminal D-alanine in the tetrapeptide moiety in peptidoglycan. This cleaves the bond between an L- and a D-amino acid. The function of this activity is in murein recycling. This family also includes the microcin c7 self-immunity protein Swiss:Q47511. This family corresponds to Merops family S66.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Peptidase S66	hydrolase activity catalytic activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR029062	Class I glutamine amidotransferase-like	Homologous Superfamily
A, B, C, D	IPR040921	LD-carboxypeptidase, C-terminal	Domain
A, B, C, D	IPR027461	LD-carboxypeptidase A, C-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR040449	LD-carboxypeptidase, N-terminal	Domain
A, B, C, D	IPR027478	Murein tetrapeptide carboxypeptidase, N-terminal	Homologous Superfamily
A, B, C, D	IPR003507	Peptidase family S66	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.