CRYSTAL STRUCTURE OF NADH-CYTOCHROME B5 REDUCTASE FROM PIG LIVER AT 2.4 ANGSTROMS RESOLUTION
External Resource: Annotation
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Chains | Domain Info | Class | Fold | Superfamily | Family | Domain | Species | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | d1ndha1 | All beta proteins | Reductase/isomerase/elongation factor common domain | Riboflavin synthase domain-like | Ferredoxin reductase FAD-binding domain-like | cytochrome b5 reductase | pig (Sus scrofa ) [TaxId: 9823 ], | SCOPe (2.08) |
A | d1ndha2 | Alpha and beta proteins (a/b) | Ferredoxin reductase-like, C-terminal NADP-linked domain | Ferredoxin reductase-like, C-terminal NADP-linked domain | Reductases | cytochrome b5 reductase | pig (Sus scrofa ) [TaxId: 9823 ], | SCOPe (2.08) |
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
A | SCOP2 Family | Ferredoxin reductase FAD-binding domain-like | 8029678 | 4002840 | SCOP2 (2022-06-29) |
A | SCOP2 Family | Reductases | 8031816 | 4003770 | SCOP2 (2022-06-29) |
A | SCOP2 Superfamily | Riboflavin synthase domain-like | 8042057 | 3001812 | SCOP2 (2022-06-29) |
A | SCOP2 Superfamily | Ferredoxin reductase-like, C-terminal NADP-linked domain | 8044194 | 3001461 | SCOP2 (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 | FAD_binding_6 | e1ndhA1 | A: beta barrels | X: cradle loop barrel | H: RIFT-related | T: Alanine racemase-C | F: FAD_binding_6 | ECOD (1.6) |
A | NAD_binding_1 | e1ndhA2 | A: a/b three-layered sandwiches | X: Ferredoxin reductase-like, C-terminal NADP-linked domain (From Topology) | H: Ferredoxin reductase-like, C-terminal NADP-linked domain (From Topology) | T: Ferredoxin reductase-like, C-terminal NADP-linked domain | F: NAD_binding_1 | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
A | 2.40.30.10 | Mainly Beta | Beta Barrel | Elongation Factor Tu (Ef-tu) | domain 3 | CATH (4.3.0) |
A | 3.40.50.80 | Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF00175 | Oxidoreductase NAD-binding domain (NAD_binding_1) | Oxidoreductase NAD-binding domain | Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity. | Domain | |
PF00970 | Oxidoreductase FAD-binding domain (FAD_binding_6) | Oxidoreductase FAD-binding domain | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR001709 | Flavoprotein pyridine nucleotide cytochrome reductase | Domain | |
IPR001433 | Oxidoreductase FAD/NAD(P)-binding | Domain | |
IPR001834 | NADH:cytochrome b5 reductase-like | Family | |
IPR039261 | Ferredoxin-NADP reductase (FNR), nucleotide-binding domain | Homologous Superfamily | |
IPR008333 | Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain | Domain | |
IPR017938 | Riboflavin synthase-like beta-barrel | Homologous Superfamily | |
IPR017927 | FAD-binding domain, ferredoxin reductase-type | Domain |
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage
Chains | Enzyme Name | Description | Catalytic Residues |
---|---|---|---|
cytochrome-b5 reductase M-CSA #862 | NADH:cytochrome b5 reductase (CBR) serves as electron donor for cytochrome b5, a ubiquitous electron carrier, thus participating in a variety of metabolic pathways (including steroid biosynthesis, desaturation and elongation of fatty acids, P450-dependent reactions, methaemoglobin reduction, etc.). | EC: 1.6.2.2 (PDB Primary Data) |