6ISN

Phosphoglycerate mutase 1 complexed with a small molecule inhibitor

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
Pharos: Disease Associations
Protein Modification Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A [auth B]	d6isnb_	Alpha and beta proteins (a/b)	Phosphoglycerate mutase-like	Phosphoglycerate mutase-like	Cofactor-dependent phosphoglycerate mutase	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B [auth C]	d6isnc_	Alpha and beta proteins (a/b)	Phosphoglycerate mutase-like	Phosphoglycerate mutase-like	Cofactor-dependent phosphoglycerate mutase	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth B]	SCOP2B Superfamily	Histidine phosphatase-like	8070063	3000781	SCOP2B (2022-06-29)
B [auth C]	SCOP2B Superfamily	Histidine phosphatase-like	8070063	3000781	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 [auth B]	His_Phos_1	e6isnB1	A: a/b three-layered sandwiches	X: Phosphoglycerate mutase-like (From Topology)	H: Phosphoglycerate mutase-like (From Topology)	T: Phosphoglycerate mutase-like	F: His_Phos_1	ECOD (1.6)
B [auth C]	His_Phos_1	e6isnC1	A: a/b three-layered sandwiches	X: Phosphoglycerate mutase-like (From Topology)	H: Phosphoglycerate mutase-like (From Topology)	T: Phosphoglycerate mutase-like	F: His_Phos_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth B]	3.40.50.1240	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Phosphoglycerate mutase-like	CATH (utative)
B [auth C]	3.40.50.1240	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Phosphoglycerate mutase-like	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth B], B [auth C]	PF00300	Histidine phosphatase superfamily (branch 1) (His_Phos_1)	Histidine phosphatase superfamily (branch 1)	The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the p ...	The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B], B [auth C]	Phosphoglycerate mutase 1	protein binding binding kinase binding enzyme binding protein kinase binding hydrolase activity catalytic activity bisphosphoglycerate mutase activity isomerase activity intramolecular phosphotransferase activity intramolecular transferase activity 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity phosphoglycerate mutase activity	monosaccharide metabolic process carbohydrate metabolic process small molecule biosynthetic process carbohydrate biosynthetic process hexose metabolic process primary metabolic process monosaccharide biosynthetic process gluconeogenesis hexose biosynthetic process biosynthetic process small molecule metabolic process metabolic process glucose metabolic process ribonucleotide catabolic process monosaccharide metabolic process carbohydrate metabolic process small molecule biosynthetic process carbohydrate biosynthetic process hexose metabolic process primary metabolic process monosaccharide biosynthetic process gluconeogenesis hexose biosynthetic process biosynthetic process small molecule metabolic process metabolic process glucose metabolic 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 NADH regeneration purine ribonucleotide catabolic process phosphorus metabolic process glucose catabolic process to pyruvate pyridine nucleotide metabolic process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process pyruvate metabolic process hexose catabolic process cellular metabolic process purine nucleoside diphosphate metabolic process purine-containing compound catabolic process nucleotide metabolic process NADH metabolic process nucleobase-containing compound catabolic process nucleoside diphosphate metabolic process purine nucleoside diphosphate catabolic process glucose catabolic process nucleoside diphosphate catabolic process nucleoside triphosphate metabolic process monocarboxylic acid metabolic process purine ribonucleotide metabolic process monosaccharide catabolic process small molecule catabolic process pyridine-containing compound catabolic process ribose phosphate metabolic process canonical glycolysis catabolic process ATP metabolic process NAD metabolic process glycolytic process through glucose-6-phosphate NAD catabolic 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 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 glycolytic process through fructose-6-phosphate	membrane cellular anatomical entity extracellular region extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle organelle extracellular space vesicle extracellular membrane-bounded organelle vesicle lumen intracellular anatomical structure intracellular vesicle membrane cellular anatomical entity extracellular region extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle organelle extracellular space vesicle extracellular membrane-bounded organelle vesicle lumen intracellular anatomical structure intracellular vesicle membrane-enclosed lumen cytoplasmic vesicle lumen secretory granule lumen intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen intracellular organelle cytoplasmic vesicle organelle lumen secretory granule secretory vesicle cytoplasm cytosol ficolin-1-rich granule ficolin-1-rich granule lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], B [auth C]	IPR013078	Histidine phosphatase superfamily, clade-1	Family
A [auth B], B [auth C]	IPR001345	Phosphoglycerate/bisphosphoglycerate mutase, active site	Active Site
A [auth B], B [auth C]	IPR029033	Histidine phosphatase superfamily	Homologous Superfamily
A [auth B], B [auth C]	IPR005952	Phosphoglycerate mutase 1	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A [auth B], B [auth C]	Pharos: P18669	squamous cell carcinoma non-small cell lung carcinoma adenocarcinoma carcinoma granular cell carcinoma Mammary Neoplasms, Experimental tubular adenocarcinoma sarcomatoid carcinoma cribriform carcinoma of breast oral cavity neoplasm gastric cancer hereditary diffuse gastric adenocarcinoma undifferentiated carcinoma bipolar disorder cribriform carcinoma squamous cell carcinoma non-small cell lung carcinoma adenocarcinoma carcinoma granular cell carcinoma Mammary Neoplasms, Experimental tubular adenocarcinoma sarcomatoid carcinoma cribriform carcinoma of breast oral cavity neoplasm gastric cancer hereditary diffuse gastric adenocarcinoma undifferentiated carcinoma bipolar disorder cribriform carcinoma gastric neoplasm mammary neoplasms, animal

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A [auth B], B [auth C]	NEP	Parent Component: HIS RESID: AA0035 PSI-MOD : 1'-phospho-L-histidine MOD:00044

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.