4OJ8 | pdb_00004oj8

Crystal structure of carbapenem synthase in complex with (3S,5S)-carbapenam

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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)
C	d4oj8c1	All beta proteins	Double-stranded beta-helix	Clavaminate synthase-like	gamma-Butyrobetaine hydroxylase	Carbapenem synthase, CarC	(Pectobacterium carotovorum subsp. carotovorum ) [TaxId: 555 ],	SCOPe (2.08)
C	d4oj8c2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Pectobacterium carotovorum subsp. carotovorum ) [TaxId: 555 ],	SCOPe (2.08)
B	d4oj8b1	All beta proteins	Double-stranded beta-helix	Clavaminate synthase-like	gamma-Butyrobetaine hydroxylase	Carbapenem synthase, CarC	(Pectobacterium carotovorum subsp. carotovorum ) [TaxId: 555 ],	SCOPe (2.08)
B	d4oj8b2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Pectobacterium carotovorum subsp. carotovorum ) [TaxId: 555 ],	SCOPe (2.08)
A	d4oj8a1	All beta proteins	Double-stranded beta-helix	Clavaminate synthase-like	gamma-Butyrobetaine hydroxylase	Carbapenem synthase, CarC	(Pectobacterium carotovorum subsp. carotovorum ) [TaxId: 555 ],	SCOPe (2.08)
A	d4oj8a2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Pectobacterium carotovorum subsp. carotovorum ) [TaxId: 555 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C	SCOP2B Superfamily	Clavaminate synthase-like	8033697	3001848	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Clavaminate synthase-like	8033697	3001848	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Clavaminate synthase-like	8033697	3001848	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)
C	TauD	e4oj8C1	A: beta sandwiches	X: jelly-roll	H: Double-stranded beta-helix (From Topology)	T: Double-stranded beta-helix	F: TauD	ECOD (1.6)
B	TauD	e4oj8B1	A: beta sandwiches	X: jelly-roll	H: Double-stranded beta-helix (From Topology)	T: Double-stranded beta-helix	F: TauD	ECOD (1.6)
A	TauD	e4oj8A1	A: beta sandwiches	X: jelly-roll	H: Double-stranded beta-helix (From Topology)	T: Double-stranded beta-helix	F: TauD	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	3.60.130.10	Alpha Beta	4-Layer Sandwich	Double-stranded beta-helix	Clavaminate synthase-like	CATH (4.3.0)
B	3.60.130.10	Alpha Beta	4-Layer Sandwich	Double-stranded beta-helix	Clavaminate synthase-like	CATH (4.3.0)
A	3.60.130.10	Alpha Beta	4-Layer Sandwich	Double-stranded beta-helix	Clavaminate synthase-like	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	(5R)-carbapenem-3-carboxylate synthase	oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen 2-oxoglutarate-dependent dioxygenase activity catalytic activity dioxygenase activity cation binding ion binding binding metal ion binding small molecule binding	antibiotic metabolic process biosynthetic process metabolic process cellular process antibiotic biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR003819	TauD/TfdA-like domain	Domain
A, B, C	IPR050411	Alpha-ketoglutarate-dependent hydroxylases	Family
A, B, C	IPR042098	Glutarate 2-hydroxylase superfamily	Homologous Superfamily

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.