Annotations: 1ZNQ

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A [auth O]	d1znqo1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domain	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A [auth O]	d1znqo2	Alpha and beta proteins (a+b)	FwdE/GAPDH domain-like	Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain	GAPDH-like	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B [auth P]	d1znqp1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domain	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B [auth P]	d1znqp2	Alpha and beta proteins (a+b)	FwdE/GAPDH domain-like	Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain	GAPDH-like	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C [auth R]	d1znqr1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domain	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C [auth R]	d1znqr2	Alpha and beta proteins (a+b)	FwdE/GAPDH domain-like	Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain	GAPDH-like	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D [auth Q]	d1znqq1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domain	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D [auth Q]	d1znqq2	Alpha and beta proteins (a+b)	FwdE/GAPDH domain-like	Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain	GAPDH-like	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)	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 O]	SCOP2B Superfamily	GAPDH-like	8044622	3000043	SCOP2B (2022-06-29)
B [auth P]	SCOP2B Superfamily	GAPDH-like	8044622	3000043	SCOP2B (2022-06-29)
C [auth R]	SCOP2B Superfamily	GAPDH-like	8044622	3000043	SCOP2B (2022-06-29)
D [auth Q]	SCOP2B Superfamily	GAPDH-like	8044622	3000043	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 O]	PF02800	e1znqO1	A: a+b two layers	X: FwdE/GAPDH domain-like	H: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain (From Topology)	T: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain	F: PF02800	ECOD (1.6)
A [auth O]	PF00044	e1znqO2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: PF00044	ECOD (1.6)
B [auth P]	PF02800	e1znqP1	A: a+b two layers	X: FwdE/GAPDH domain-like	H: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain (From Topology)	T: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain	F: PF02800	ECOD (1.6)
B [auth P]	PF00044	e1znqP2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: PF00044	ECOD (1.6)
C [auth R]	PF02800	e1znqR1	A: a+b two layers	X: FwdE/GAPDH domain-like	H: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain (From Topology)	T: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain	F: PF02800	ECOD (1.6)
C [auth R]	PF00044	e1znqR2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: PF00044	ECOD (1.6)
D [auth Q]	PF02800	e1znqQ1	A: a+b two layers	X: FwdE/GAPDH domain-like	H: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain (From Topology)	T: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain	F: PF02800	ECOD (1.6)
D [auth Q]	PF00044	e1znqQ2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: PF00044	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth O]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
A [auth O]	3.30.360.10	Alpha Beta	2-Layer Sandwich	Dihydrodipicolinate Reductase	domain 2	CATH (4.3.0)
B [auth P]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
B [auth P]	3.30.360.10	Alpha Beta	2-Layer Sandwich	Dihydrodipicolinate Reductase	domain 2	CATH (4.3.0)
C [auth R]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
C [auth R]	3.30.360.10	Alpha Beta	2-Layer Sandwich	Dihydrodipicolinate Reductase	domain 2	CATH (4.3.0)
D [auth Q]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
D [auth Q]	3.30.360.10	Alpha Beta	2-Layer Sandwich	Dihydrodipicolinate Reductase	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth O], B [auth P], C [auth R], D [auth Q]	PF02800	Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain (Gp_dh_C)	Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain	GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.	Domain
A [auth O], B [auth P], C [auth R], D [auth Q]	PF00044	Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain (Gp_dh_N)	Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain	GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth O], B [auth P], C [auth R], D [auth Q]	Glyceraldehyde-3-phosphate dehydrogenase, liver	cytoskeletal protein binding microtubule binding protein binding binding tubulin binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding small molecule binding transferase activity, transferring nitrogenous groups cytoskeletal protein binding microtubule binding protein binding binding tubulin binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding small molecule binding transferase activity, transferring nitrogenous groups catalytic activity, acting on a protein peptidyl-cysteine S-nitrosylase activity transferase activity catalytic activity enzyme regulator activity molecular function inhibitor activity peptidase regulator activity molecular function regulator activity enzyme inhibitor activity aspartic-type endopeptidase inhibitor activity peptidase inhibitor activity endopeptidase regulator activity endopeptidase inhibitor activity glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor NAD binding disordered domain specific binding protein domain specific binding identical protein binding	cellular response to stimulus positive regulation of cell communication regulation of cellular process positive regulation of signal transduction positive regulation of canonical NF-kappaB signal transduction response to stimulus signaling positive regulation of biological process regulation of signal transduction intracellular signal transduction cell communication positive regulation of response to stimulus regulation of intracellular signal transduction intracellular signaling cassette cellular response to stimulus positive regulation of cell communication regulation of cellular process positive regulation of signal transduction positive regulation of canonical NF-kappaB signal transduction response to stimulus signaling positive regulation of biological process regulation of signal transduction intracellular signal transduction cell communication positive regulation of response to stimulus regulation of intracellular signal transduction intracellular signaling cassette signal transduction positive regulation of cellular process regulation of biological process regulation of signaling biological regulation positive regulation of intracellular signal transduction canonical NF-kappaB signal transduction regulation of response to stimulus regulation of cell communication regulation of canonical NF-kappaB signal transduction cellular process positive regulation of signaling cellular biosynthetic process organonitrogen compound biosynthetic process negative regulation of biological process negative regulation of cellular metabolic process regulation of primary metabolic process post-transcriptional regulation of gene expression negative regulation of translation organic substance metabolic process organic substance biosynthetic process negative regulation of cellular process protein metabolic process negative regulation of protein metabolic process negative regulation of macromolecule metabolic process regulation of biosynthetic process organonitrogen compound metabolic process cellular metabolic process regulation of protein metabolic process negative regulation of metabolic process regulation of cellular metabolic process primary metabolic process regulation of macromolecule metabolic process gene expression translation macromolecule biosynthetic process negative regulation of cellular biosynthetic process regulation of cellular biosynthetic process regulation of gene expression negative regulation of gene expression biosynthetic process negative regulation of biosynthetic process regulation of translation negative regulation of macromolecule biosynthetic process regulation of macromolecule biosynthetic process metabolic process macromolecule metabolic process regulation of metabolic process regulation of protein stability regulation of biological quality protein stabilization catabolic process macroautophagy autophagy regulation of catabolic process regulation of autophagy cellular catabolic process regulation of macroautophagy regulation of cellular catabolic process process utilizing autophagic mechanism monosaccharide metabolic process carbohydrate metabolic process hexose metabolic process small molecule 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 purine ribonucleotide catabolic process phosphorus metabolic process pyridine nucleotide metabolic process nucleoside phosphate metabolic process organonitrogen compound catabolic process nicotinamide nucleotide metabolic process pyruvate metabolic process purine nucleoside diphosphate metabolic process purine-containing compound catabolic process nucleotide metabolic process nucleobase-containing compound catabolic process organic cyclic compound metabolic process nucleoside diphosphate metabolic process purine nucleoside diphosphate catabolic process nucleoside diphosphate catabolic process nucleoside triphosphate metabolic process monocarboxylic acid metabolic process purine ribonucleotide metabolic process pyridine-containing compound catabolic process ribose phosphate metabolic 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 derivative catabolic process ADP catabolic process carboxylic acid metabolic process generation of precursor metabolites and energy organic cyclic compound catabolic process purine-containing compound metabolic process ADP metabolic process organophosphate metabolic process purine ribonucleoside diphosphate metabolic process organic substance catabolic process purine ribonucleoside diphosphate catabolic process negative regulation of hydrolase activity negative regulation of proteolysis regulation of catalytic activity negative regulation of catalytic activity negative regulation of endopeptidase activity negative regulation of peptidase activity regulation of proteolysis proteolysis regulation of endopeptidase activity regulation of peptidase activity negative regulation of molecular function regulation of molecular function regulation of hydrolase activity response to organic substance biological process involved in interspecies interaction between organisms response to type II interferon response to cytokine cellular response to type II interferon response to biotic stimulus response to stress innate immune response cellular response to cytokine stimulus response to external biotic stimulus cellular response to organic substance immune response response to other organism defense response defense response to symbiont response to external stimulus cellular response to chemical stimulus response to chemical immune system process defense response to other organism peptidyl-cysteine modification peptidyl-cysteine S-nitrosylation peptidyl-cysteine S-trans-nitrosylation macromolecule modification peptidyl-amino acid modification protein modification process protein nitrosylation disruption of cell in another organism biological process involved in symbiotic interaction killing by host of symbiont cells disruption of anatomical structure in another organism biological process involved in interaction with symbiont killing of cells of another organism cell killing neuron apoptotic process apoptotic process cell death programmed cell death humoral immune response antimicrobial humoral response antimicrobial humoral immune response mediated by antimicrobial peptide defense response to fungus response to fungus cellular component organization organelle organization microtubule cytoskeleton organization microtubule-based process cellular component organization or biogenesis cytoskeleton organization multicellular organismal process positive regulation of cellular metabolic process positive regulation of macromolecule biosynthetic process positive regulation of metabolic process positive regulation of biosynthetic process cytokine production regulation of cytokine production regulation of multicellular organismal process positive regulation of macromolecule metabolic process positive regulation of gene expression positive regulation of multicellular organismal process positive regulation of cytokine production positive regulation of cellular biosynthetic process positive regulation of type I interferon production type I interferon production regulation of type I interferon production	membrane cellular anatomical entity membrane-bounded organelle organelle vesicle intracellular anatomical structure nuclear membrane nucleus intracellular membrane-bounded organelle endomembrane system intracellular organelle organelle envelope nuclear envelope organelle membrane membrane cellular anatomical entity membrane-bounded organelle organelle vesicle intracellular anatomical structure nuclear membrane nucleus intracellular membrane-bounded organelle endomembrane system intracellular organelle organelle envelope nuclear envelope organelle membrane extracellular exosome extracellular vesicle extracellular organelle extracellular region extracellular space extracellular membrane-bounded organelle cytoplasm cytosol protein-containing complex GAIT complex cell periphery plasma membrane cytoskeleton intracellular non-membrane-bounded organelle microtubule cytoskeleton non-membrane-bounded organelle lipid droplet perinuclear region of cytoplasm ribonucleoprotein complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth O], B [auth P], C [auth R], D [auth Q]	IPR020830	Glyceraldehyde 3-phosphate dehydrogenase, active site	Active Site
A [auth O], B [auth P], C [auth R], D [auth Q]	IPR020831	Glyceraldehyde/Erythrose phosphate dehydrogenase family	Family
A [auth O], B [auth P], C [auth R], D [auth Q]	IPR020828	Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain	Domain
A [auth O], B [auth P], C [auth R], D [auth Q]	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A [auth O], B [auth P], C [auth R], D [auth Q]	IPR020829	Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain	Domain
A [auth O], B [auth P], C [auth R], D [auth Q]	IPR006424	Glyceraldehyde-3-phosphate dehydrogenase, type I	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A [auth O], B [auth P], C [auth R], D [auth Q]	Pharos: P04406	squamous cell carcinoma acute coronary syndrome Hypoxia colorectal cancer osteoporosis esophageal cancer lung adenocarcinoma ovarian disease eye disease hematologic disease urinary bladder disease lung cancer lymphoplasmacytic lymphoma atherosclerosis neurodegenerative disease squamous cell carcinoma acute coronary syndrome Hypoxia colorectal cancer osteoporosis esophageal cancer lung adenocarcinoma ovarian disease eye disease hematologic disease urinary bladder disease lung cancer lymphoplasmacytic lymphoma atherosclerosis neurodegenerative disease cancer oral cavity neoplasm colonic disease pancreatic ductal adenocarcinoma glioblastoma hepatocellular carcinoma prostate disease stomach disease liver disease uterine disease lung disease autoimmune disease non-small cell lung carcinoma cerebrovascular disorder osteoarthritis coronary artery disease ovarian cancer plasma cell myeloma heart disease hypertensive disorder skin disease kidney disease type 2 diabetes mellitus vertebral column disease lymphatic system disease malignant pancreatic neoplasm arthritic joint disease neoplasm of esophagus breast disease obesity disorder osteoarthritis susceptibility 1 colorectal carcinoma

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.