2ZMA

Crystal Structure of 6-Aminohexanoate-dimer Hydrolase S112A/G181D/H266N/D370Y Mutant with Substrate

External Resource: Annotation

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2zmaa_	Multi-domain proteins (alpha and beta)	beta-lactamase/transpeptidase-like	beta-lactamase/transpeptidase-like	beta-Lactamase/D-ala carboxypeptidase	6-aminohexanoate-dimer hydrolase NylC	(Flavobacterium sp. ) [TaxId: 239 ], (Flavobacterium sp. ) [TaxId: 239 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Beta-lactamase_1st	e2zmaA1	A: alpha complex topology	X: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology)	H: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology)	T: alpha-helical domain in beta-lactamase/transpeptidase-like proteins	F: Beta-lactamase_1st	ECOD (1.6)
A	Beta-lactamase_2nd_1	e2zmaA2	A: a+b three layers	X: Profilin-like	H: a+b domain in beta-lactamase/transpeptidase-like proteins (From Topology)	T: a+b domain in beta-lactamase/transpeptidase-like proteins	F: Beta-lactamase_2nd_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	6.10.250.420	Special	Helix non-globular	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		CATH (4.3.0)
A	3.40.710.10	Alpha Beta	3-Layer(aba) Sandwich	Beta-lactamase	DD-peptidase/beta-lactamase superfamily	CATH (4.3.0)
A	1.20.58.710	Mainly Alpha	Up-down Bundle	Methane Monooxygenase Hydroxylase	Chain G, domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00144	Beta-lactamase (Beta-lactamase)	Beta-lactamase	This family appears to be distantly related to Pfam:PF00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	6-aminohexanoate-dimer hydrolase	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides hydrolase activity 6-aminohexanoate-dimer hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds	nylon catabolic process cellular response to stimulus catabolic process response to stimulus cellular response to xenobiotic stimulus cellular metabolic process xenobiotic catabolic process xenobiotic metabolic process response to xenobiotic stimulus cellular catabolic process cellular response to chemical stimulus nylon metabolic process response to chemical cellular process nylon catabolic process cellular response to stimulus catabolic process response to stimulus cellular response to xenobiotic stimulus cellular metabolic process xenobiotic catabolic process xenobiotic metabolic process response to xenobiotic stimulus cellular catabolic process cellular response to chemical stimulus nylon metabolic process response to chemical cellular process metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR001466	Beta-lactamase-related	Domain
A	IPR012338	Beta-lactamase/transpeptidase-like	Homologous Superfamily
A	IPR050789	Diverse Enzymatic Activities	Family
A	IPR001466	Beta-lactamase-related	Domain
A	IPR012338	Beta-lactamase/transpeptidase-like	Homologous Superfamily
A	IPR050789	Diverse Enzymatic Activities	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.