2XVZ

Cobalt chelatase CbiK (periplasmatic) from Desulvobrio vulgaris Hildenborough (co-crystallized with cobalt)

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 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	d2xvza_	Alpha and beta proteins (a/b)	Chelatase-like	Chelatase	automated matches	automated matches	(Nitratidesulfovibrio vulgaris str. Hildenborough ) [TaxId: 882 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Cobalt chelatase CbiK	8084412	4000840	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Chelatase	8084413	3001656	SCOP2 (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	CbiK	e2xvzA1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Chelatase-like	F: CbiK	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1400	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF06180	Cobalt chelatase (CbiK) (CbiK)	Cobalt chelatase (CbiK)	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	CHELATASE, PUTATIVE	cation binding transition metal ion binding ion binding binding metal ion binding cobalt ion binding small molecule binding sirohydrochlorin ferrochelatase activity lyase activity ferrochelatase activity catalytic activity organic cyclic compound binding tetrapyrrole binding heme binding cation binding transition metal ion binding ion binding binding metal ion binding cobalt ion binding small molecule binding sirohydrochlorin ferrochelatase activity lyase activity ferrochelatase activity catalytic activity organic cyclic compound binding tetrapyrrole binding heme binding sirohydrochlorin cobaltochelatase activity	cobalamin metabolic process cobalamin biosynthetic process water-soluble vitamin biosynthetic process tetrapyrrole metabolic process anaerobic cobalamin biosynthetic process small molecule biosynthetic process cellular biosynthetic process cellular metabolic process vitamin biosynthetic process vitamin metabolic process tetrapyrrole biosynthetic process biosynthetic process small molecule metabolic process metabolic process cobalamin metabolic process cobalamin biosynthetic process water-soluble vitamin biosynthetic process tetrapyrrole metabolic process anaerobic cobalamin biosynthetic process small molecule biosynthetic process cellular biosynthetic process cellular metabolic process vitamin biosynthetic process vitamin metabolic process tetrapyrrole biosynthetic process biosynthetic process small molecule metabolic process metabolic process cellular process water-soluble vitamin metabolic process cellular component organization cellular component biogenesis cellular component assembly protein-containing complex organization protein complex oligomerization protein tetramerization protein-containing complex assembly cellular component organization or biogenesis	periplasmic space cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR010388	Anaerobic cobalt chelatase	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.