3NBU | pdb_00003nbu

Crystal structure of pGI glucosephosphate isomerase

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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	d3nbua_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	Phosphoglucose isomerase, PGI	automated matches	(Escherichia coli DH5[alpha] ) [TaxId: 668369 ],	SCOPe (2.08)
B	d3nbub_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	Phosphoglucose isomerase, PGI	automated matches	(Escherichia coli DH5[alpha] ) [TaxId: 668369 ],	SCOPe (2.08)
C	d3nbuc_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	Phosphoglucose isomerase, PGI	automated matches	(Escherichia coli DH5[alpha] ) [TaxId: 668369 ],	SCOPe (2.08)
D	d3nbud_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	Phosphoglucose isomerase, PGI	automated matches	(Escherichia coli DH5[alpha] ) [TaxId: 668369 ],	SCOPe (2.08)
E	d3nbue_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	Phosphoglucose isomerase, PGI	automated matches	(Escherichia coli DH5[alpha] ) [TaxId: 668369 ],	SCOPe (2.08)
F	d3nbuf_	Alpha and beta proteins (a/b)	SIS domain	SIS domain	Phosphoglucose isomerase, PGI	automated matches	(Escherichia coli DH5[alpha] ) [TaxId: 668369 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PGI_N	e3nbuA2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: PGI_N	ECOD (1.6)
A	PGI_C	e3nbuA1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: PGI_C	ECOD (1.6)
B	PGI_N	e3nbuB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: PGI_N	ECOD (1.6)
B	PGI_C	e3nbuB2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: PGI_C	ECOD (1.6)
C	PGI_N	e3nbuC1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: PGI_N	ECOD (1.6)
C	PGI_C	e3nbuC2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: PGI_C	ECOD (1.6)
D	PGI_N	e3nbuD1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: PGI_N	ECOD (1.6)
D	PGI_C	e3nbuD2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: PGI_C	ECOD (1.6)
E	PGI_N	e3nbuE1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: PGI_N	ECOD (1.6)
E	PGI_C	e3nbuE2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: PGI_C	ECOD (1.6)
F	PGI_N	e3nbuF1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: PGI_N	ECOD (1.6)
F	PGI_C	e3nbuF2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Ribosomal protein S2/SIS domain (From Topology)	T: Ribosomal protein S2/SIS domain	F: PGI_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
A	1.10.1390.10	Mainly Alpha	Orthogonal Bundle	Phosphoglucose isomerase, C-terminal domain		CATH (4.3.0)
B	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
B	1.10.1390.10	Mainly Alpha	Orthogonal Bundle	Phosphoglucose isomerase, C-terminal domain		CATH (4.3.0)
C	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
C	1.10.1390.10	Mainly Alpha	Orthogonal Bundle	Phosphoglucose isomerase, C-terminal domain		CATH (4.3.0)
D	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
D	1.10.1390.10	Mainly Alpha	Orthogonal Bundle	Phosphoglucose isomerase, C-terminal domain		CATH (4.3.0)
E	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
E	1.10.1390.10	Mainly Alpha	Orthogonal Bundle	Phosphoglucose isomerase, C-terminal domain		CATH (4.3.0)
F	3.40.50.10490	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glucose-6-phosphate isomerase like protein	CATH (4.3.0)
F	1.10.1390.10	Mainly Alpha	Orthogonal Bundle	Phosphoglucose isomerase, C-terminal domain		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF00342	Phosphoglucose isomerase (PGI)	Phosphoglucose isomerase	Phosphoglucose isomerase catalyses the interconversion of glucose-6-phosphate and fructose-6-phosphate.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	Glucose-6-phosphate isomerase	identical protein binding protein binding binding protein homodimerization activity protein dimerization activity isomerase activity intramolecular oxidoreductase activity, interconverting aldoses and ketoses intramolecular oxidoreductase activity glucose-6-phosphate isomerase activity catalytic activity carbohydrate derivative binding monosaccharide binding carbohydrate binding small molecule binding	ribonucleotide catabolic process pyridine nucleotide catabolic process aerobic respiration 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 ribonucleotide catabolic process pyridine nucleotide catabolic process aerobic respiration 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 nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process pyruvate 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 cellular respiration catabolic process ATP metabolic process energy derivation by oxidation of organic compounds 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 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 small molecule biosynthetic process carbohydrate biosynthetic process hexose metabolic process monosaccharide biosynthetic process gluconeogenesis hexose biosynthetic process biosynthetic process glucose metabolic process glucose 6-phosphate metabolic process cellular response to stimulus response to oxidative stress cellular response to chemical stimulus response to stimulus cellular response to stress response to stress response to chemical cellular response to oxidative stress cellular response to chemical stress	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR046348	SIS domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR035476	Phosphoglucose isomerase, SIS domain 1	Domain
A, B, C, D, E A, B, C, D, E, F	IPR018189	Phosphoglucose isomerase, conserved site	Conserved Site
A, B, C, D, E A, B, C, D, E, F	IPR035482	Phosphoglucose isomerase, SIS domain 2	Domain
A, B, C, D, E A, B, C, D, E, F	IPR001672	Phosphoglucose isomerase (PGI)	Family
A, B, C, D, E A, B, C, D, E, F	IPR023096	Phosphoglucose isomerase, C-terminal	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.