7B3R | pdb_00007b3r

OXA-10 beta-lactamase with S64Dha modification and lysinoalanine crosslink

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
AMR Gene: CARD Annotation
AMR Gene Family: CARD Annotation
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	beta-lactamase/transpeptidase-like	8037816	3001604	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	beta-lactamase/transpeptidase-like	8037816	3001604	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	Transpeptidase_1st	e7b3rA2	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: Transpeptidase_1st	ECOD (1.6)
A	Transpeptidase_2nd_1	e7b3rA1	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: Transpeptidase_2nd_1	ECOD (1.6)
B	Transpeptidase_1st	e7b3rB1	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: Transpeptidase_1st	ECOD (1.6)
B	Transpeptidase_2nd_1	e7b3rB2	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: Transpeptidase_2nd_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.710.10	Alpha Beta	3-Layer(aba) Sandwich	Beta-lactamase	DD-peptidase/beta-lactamase superfamily	CATH (utative)

AMR Gene: CARD Annotation CARD Database Homepage

Chains	Accession	Short Name	Description	Provenance Source (Version)
A	ARO:3001405	OXA-10	OXA-10 is a beta-lactamase found in Acinetobacter baumannii and P. aeruginosa.	CARD (4.0.0)
A	ARO:3001405	OXA-10	OXA-10 is a beta-lactamase found in Acinetobacter baumannii and P. aeruginosa.	CARD (4.0.0)
B	ARO:3001405	OXA-10	OXA-10 is a beta-lactamase found in Acinetobacter baumannii and P. aeruginosa.	CARD (4.0.0)
B	ARO:3001405	OXA-10	OXA-10 is a beta-lactamase found in Acinetobacter baumannii and P. aeruginosa.	CARD (4.0.0)

AMR Gene Family: CARD Annotation CARD Database Homepage

Chains	Accession	Gene Family	Drug Class	Resistance Machanism	Provenance Source (Version)
A	ARO:3007697	OXA-10-like beta-lactamase	cephalosporin, penicillin beta-lactam	antibiotic inactivation	CARD (4.0.0)
A	ARO:3007697	OXA-10-like beta-lactamase	cephalosporin, penicillin beta-lactam	antibiotic inactivation	CARD (4.0.0)
B	ARO:3007697	OXA-10-like beta-lactamase	cephalosporin, penicillin beta-lactam	antibiotic inactivation	CARD (4.0.0)
B	ARO:3007697	OXA-10-like beta-lactamase	cephalosporin, penicillin beta-lactam	antibiotic inactivation	CARD (4.0.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00905	Penicillin binding protein transpeptidase domain (Transpeptidase)	Penicillin binding protein transpeptidase domain	The active site serine (residue 337 in Swiss:P14677) is conserved in all members of this family.	Domain
B	PF00905	Penicillin binding protein transpeptidase domain (Transpeptidase)	Penicillin binding protein transpeptidase domain	The active site serine (residue 337 in Swiss:P14677) is conserved in all members of this family.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Beta-lactamase OXA-10	amide binding organic acid binding binding ion binding anion binding penicillin binding carboxylic acid binding heterocyclic compound binding monocarboxylic acid binding small molecule binding sulfur compound binding beta-lactamase activity hydrolase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides amide binding organic acid binding binding ion binding anion binding penicillin binding carboxylic acid binding heterocyclic compound binding monocarboxylic acid binding small molecule binding sulfur compound binding beta-lactamase activity hydrolase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds	antibiotic metabolic process catabolic process metabolic process cellular process antibiotic catabolic process cellular component organization cell wall organization or biogenesis cell wall organization cellular component organization or biogenesis external encapsulating structure organization response to stimulus response to chemical response to antibiotic	cell periphery cellular anatomical structure plasma membrane membrane periplasmic space
B	Beta-lactamase OXA-10	amide binding organic acid binding binding ion binding anion binding penicillin binding carboxylic acid binding heterocyclic compound binding monocarboxylic acid binding small molecule binding sulfur compound binding beta-lactamase activity hydrolase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides amide binding organic acid binding binding ion binding anion binding penicillin binding carboxylic acid binding heterocyclic compound binding monocarboxylic acid binding small molecule binding sulfur compound binding beta-lactamase activity hydrolase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds	antibiotic metabolic process catabolic process metabolic process cellular process antibiotic catabolic process cellular component organization cell wall organization or biogenesis cell wall organization cellular component organization or biogenesis external encapsulating structure organization response to stimulus response to chemical response to antibiotic	cell periphery cellular anatomical structure plasma membrane membrane periplasmic space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR012338	Beta-lactamase/transpeptidase-like	Homologous Superfamily
A	IPR001460	Penicillin-binding protein, transpeptidase	Domain
A	IPR050515	Bacterial Transpeptidases and Beta-Lactamases	Family
A	IPR002137	Beta-lactamase, class-D active site	Active Site
B	IPR012338	Beta-lactamase/transpeptidase-like	Homologous Superfamily
B	IPR001460	Penicillin-binding protein, transpeptidase	Domain
B	IPR050515	Bacterial Transpeptidases and Beta-Lactamases	Family
B	IPR002137	Beta-lactamase, class-D active site	Active Site

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A	DHA	Parent Component: SER RESID: AA0181 PSI-MOD : dehydroalanine (Ser) MOD:00189 , dehydroalanine (Cys) MOD:00793 , dehydroalanine (Tyr) MOD:00824 , dehydroalanine MOD:01168 , dehydroalanine (Sec) MOD:01954
A	KCX	Parent Component: LYS RESID: AA0181
B	DHA	Parent Component: SER RESID: AA0181 , AA0181 PSI-MOD : dehydroalanine (Ser) MOD:00189 , dehydroalanine (Cys) MOD:00793 , dehydroalanine (Tyr) MOD:00824 , dehydroalanine MOD:01168 , dehydroalanine (Sec) MOD:01954 , dehydroalanine (Ser) MOD:00189 , dehydroalanine (Cys) MOD:00793 , dehydroalanine (Tyr) MOD:00824 , dehydroalanine MOD:01168 , dehydroalanine (Sec) MOD:01954

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.