3IGZ

Crystal structures of Leishmania mexicana phosphoglycerate mutase at low cobalt concentration

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)
A [auth B]	Metalloenzyme	e3igzB3	A: a/b three-layered sandwiches	X: Alkaline phosphatase-like (From Topology)	H: Alkaline phosphatase-like (From Topology)	T: Alkaline phosphatase-like	F: Metalloenzyme	ECOD (1.6)
A [auth B]	iPGM_N	e3igzB2	A: a/b three-layered sandwiches	X: 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain (From Topology)	H: 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain (From Topology)	T: 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain	F: iPGM_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth B]	3.40.720.10	Alpha Beta	3-Layer(aba) Sandwich	Alkaline Phosphatase, subunit A	Alkaline Phosphatase, subunit A	CATH (4.3.0)
A [auth B]	3.40.1450.10	Alpha Beta	3-Layer(aba) Sandwich	2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain	BPG-independent phosphoglycerate mutase, domain B	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth B]	PF06415	BPG-independent PGAM N-terminus (iPGM_N) (iPGM_N)	BPG-independent PGAM N-terminus (iPGM_N)	This family represents the N-terminal region of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (or phosphoglyceromutase or BPG-independent PGAM) protein (EC:5.4.2.1). The family is found in conjunction with Pfam:PF01676 (located in t ...	This family represents the N-terminal region of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (or phosphoglyceromutase or BPG-independent PGAM) protein (EC:5.4.2.1). The family is found in conjunction with Pfam:PF01676 (located in the C-terminal region of the protein).	Domain
A [auth B]	PF01676	Metalloenzyme superfamily (Metalloenzyme)	Metalloenzyme superfamily	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B]	Cofactor-independent phosphoglycerate mutase	cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity isomerase activity phosphoglycerate mutase activity intramolecular phosphotransferase activity catalytic activity intramolecular transferase activity	ribonucleotide catabolic process pyridine nucleotide catabolic process oxoacid metabolic process carbohydrate catabolic process carbohydrate derivative metabolic process organophosphate catabolic process nucleoside phosphate catabolic process organic acid metabolic process nucleobase-containing compound metabolic process glycolytic process phosphate-containing compound metabolic process pyridine-containing compound metabolic process small molecule metabolic process purine ribonucleotide catabolic process ribonucleotide catabolic process pyridine nucleotide catabolic process oxoacid metabolic process carbohydrate catabolic process carbohydrate derivative metabolic process organophosphate catabolic process nucleoside phosphate catabolic process organic acid metabolic process nucleobase-containing compound metabolic process glycolytic process phosphate-containing compound metabolic process pyridine-containing compound metabolic process small molecule metabolic process purine ribonucleotide catabolic process phosphorus metabolic process pyridine nucleotide metabolic process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process pyruvate metabolic process cellular metabolic process purine nucleoside diphosphate metabolic process primary metabolic process purine-containing compound catabolic process nucleotide metabolic process nucleobase-containing compound catabolic process nucleoside diphosphate metabolic process purine nucleoside diphosphate catabolic process nucleoside diphosphate catabolic process metabolic process nucleoside triphosphate metabolic process monocarboxylic acid metabolic process purine ribonucleotide metabolic process pyridine-containing compound catabolic process ribose phosphate metabolic process catabolic process ATP metabolic process purine nucleotide metabolic process ribonucleotide metabolic process nucleobase-containing small molecule metabolic process purine ribonucleoside triphosphate metabolic process ribonucleoside diphosphate metabolic process ribonucleoside diphosphate catabolic process nucleotide catabolic process ribonucleoside triphosphate metabolic process purine nucleoside triphosphate metabolic process purine nucleotide catabolic process carbohydrate metabolic process carbohydrate derivative catabolic process ADP catabolic process carboxylic acid metabolic process generation of precursor metabolites and energy purine-containing compound metabolic process ADP metabolic process organophosphate metabolic process purine ribonucleoside diphosphate metabolic process cellular process purine ribonucleoside diphosphate catabolic process monosaccharide metabolic process hexose catabolic process hexose metabolic process glucose catabolic process monosaccharide catabolic process small molecule catabolic process glucose metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B]	IPR011258	BPG-independent PGAM, N-terminal	Domain
A [auth B]	IPR036646	BPG-independent phosphoglycerate mutase, domain B superfamily	Homologous Superfamily
A [auth B]	IPR005995	Phosphoglycerate mutase, 2,3-bisphosphoglycerate-independent	Family
A [auth B]	IPR006124	Metalloenzyme	Domain
A [auth B]	IPR017850	Alkaline-phosphatase-like, core 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.