3CAW | pdb_00003caw

Crystal structure of o-succinylbenzoate synthase from Bdellovibrio bacteriovorus liganded with Mg

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	EUF08271	e3cawB2	A: a+b two layers	X: Enolase-N/ribosomal protein	H: Enolase N-terminal domain-like (From Topology)	T: Enolase N-terminal domain-like	F: EUF08271	ECOD (1.6)
B	MR_MLE_C	e3cawB1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: MR_MLE_C	ECOD (1.6)
A	EUF08271	e3cawA3	A: a+b two layers	X: Enolase-N/ribosomal protein	H: Enolase N-terminal domain-like (From Topology)	T: Enolase N-terminal domain-like	F: EUF08271	ECOD (1.6)
A	MR_MLE_C	e3cawA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: MR_MLE_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.30.390.10	Alpha Beta	2-Layer Sandwich	Enolase-like	domain 1	CATH (4.3.0)
B	3.20.20.120	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Enolase-like C-terminal domain	CATH (4.3.0)
A	3.30.390.10	Alpha Beta	2-Layer Sandwich	Enolase-like	domain 1	CATH (4.3.0)
A	3.20.20.120	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Enolase-like C-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF22015	O-succinylbenzoate synthase, N-terminal domain (OSBS_N)	O-succinylbenzoate synthase, N-terminal domain	This domain is found N-terminal in members of o-succinylbenzoate synthase (OSBS) family. It is also known as capping domain. In most members, this domain consists of a central three-stranded antiparallel beta-sheet packed on one side with two helices ...	This domain is found N-terminal in members of o-succinylbenzoate synthase (OSBS) family. It is also known as capping domain. In most members, this domain consists of a central three-stranded antiparallel beta-sheet packed on one side with two helices. The second helix is truncated or missing in some members of the family [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	o-succinylbenzoate synthase	lyase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding	vitamin K metabolic process small molecule biosynthetic process ketone metabolic process vitamin biosynthetic process vitamin metabolic process biosynthetic process phylloquinone biosynthetic process vitamin K biosynthetic process fat-soluble vitamin biosynthetic process metabolic process cellular process small molecule metabolic process ketone biosynthetic process menaquinone metabolic process vitamin K metabolic process small molecule biosynthetic process ketone metabolic process vitamin biosynthetic process vitamin metabolic process biosynthetic process phylloquinone biosynthetic process vitamin K biosynthetic process fat-soluble vitamin biosynthetic process metabolic process cellular process small molecule metabolic process ketone biosynthetic process menaquinone metabolic process menaquinone biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR041338	OSBS, enolase-like N-terminal domain	Domain
A, B	IPR029017	Enolase-like, N-terminal	Homologous Superfamily
A, B	IPR036849	Enolase-like, C-terminal domain 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.