Annotations: 2GH5


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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad2gh5a2 Alpha and beta proteins (a/b) FAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains Glutathione reductase, middle domain human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Ad2gh5a1 Alpha and beta proteins (a/b) FAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains Glutathione reductase, N- and C-terminal domain human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Ad2gh5a3 Alpha and beta proteins (a+b) CO dehydrogenase flavoprotein C-domain-like FAD/NAD-linked reductases, dimerisation (C-terminal) domain FAD/NAD-linked reductases, dimerisation (C-terminal) domain Glutathione reductase human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Bd2gh5b2 Alpha and beta proteins (a/b) FAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains Glutathione reductase, middle domain human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Bd2gh5b1 Alpha and beta proteins (a/b) FAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains Glutathione reductase, N- and C-terminal domain human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Bd2gh5b3 Alpha and beta proteins (a+b) CO dehydrogenase flavoprotein C-domain-like FAD/NAD-linked reductases, dimerisation (C-terminal) domain FAD/NAD-linked reductases, dimerisation (C-terminal) domain Glutathione reductase human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyGSR C-terminal domain-like 8056194 3000028 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyThioredoxin reductase-like 8001320 3000050 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyThioredoxin reductase-like 8001320 3000050 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyGSR C-terminal domain-like 8056194 3000028 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APyr_redox_dime2gh5A3 A: a+b two layersX: FAD-linked reductases, C-terminal domain-likeH: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain (From Topology)T: FAD/NAD-linked reduatases, dimerisation (C-terminal) domainF: Pyr_redox_dimECOD (1.6)
APyr_redox_2_1e2gh5A2 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: FAD/NAD(P)-binding domainF: Pyr_redox_2_1ECOD (1.6)
APyr_redox_2e2gh5A1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: FAD/NAD(P)-binding domainF: Pyr_redox_2ECOD (1.6)
BPyr_redox_dime2gh5B3 A: a+b two layersX: FAD-linked reductases, C-terminal domain-likeH: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain (From Topology)T: FAD/NAD-linked reduatases, dimerisation (C-terminal) domainF: Pyr_redox_dimECOD (1.6)
BPyr_redox_2_1e2gh5B2 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: FAD/NAD(P)-binding domainF: Pyr_redox_2_1ECOD (1.6)
BPyr_redox_2e2gh5B1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: FAD/NAD(P)-binding domainF: Pyr_redox_2ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.50.50.60 Alpha Beta 3-Layer(bba) Sandwich FAD/NAD(P)-binding domain FAD/NAD(P)-binding domainCATH (4.3.0)
A3.30.390.30 Alpha Beta 2-Layer Sandwich Enolase-like domain 1CATH (4.3.0)
B3.50.50.60 Alpha Beta 3-Layer(bba) Sandwich FAD/NAD(P)-binding domain FAD/NAD(P)-binding domainCATH (4.3.0)
B3.30.390.30 Alpha Beta 2-Layer Sandwich Enolase-like domain 1CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF00070Pyridine nucleotide-disulphide oxidoreductase (Pyr_redox)Pyridine nucleotide-disulphide oxidoreductaseThis family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.Domain
A, B
PF02852Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain (Pyr_redox_dim)Pyridine nucleotide-disulphide oxidoreductase, dimerisation domainThis family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
glutathione reductase, mitochondrial

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
A, B
glutathione-disulfide reductase  M-CSA #6

The pyrimidine nucleotide-disulphide oxidoreductases are a family of proteins which transfer electrons from NAD(P)H via FAD to a redox-active disulphide bond in the enzyme active site, which then reduces the substrate.

The structure of the ubiquitous enzyme glutathione reductase (EC 1.6.4.2), which helps protect cells from oxidative stress, is similar to trypanothione reductase (EC 1.6.4.8), lipoamide dehydrogenase (EC 1.8.1.4), higher eukaryotic thioredoxin reductase (EC 1.6.4.5) and mercuric reductase (1.16.1.1).

Defined by 7 residues: CYS:A-58CYS:A-63LYS:A-66TYR:A-197GLU:A-201HIS:B-467GLU:B-472
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Explore in 3DM-CSA Motif Definition