1TDE
CRYSTAL STRUCTURE OF ESCHERICHIA COLI THIOREDOXIN REDUCTASE REFINED AT 2 ANGSTROM RESOLUTION: IMPLICATIONS FOR A LARGE CONFORMATIONAL CHANGE DURING CATALYSIS
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 | d1tdea1 | 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 | Thioredoxin reductase | (Escherichia coli ) [TaxId: 562 ], | SCOPe (2.08) |
Domain Annotation: ECOD Classification ECOD Database Homepage
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
A | 3.50.50.60 | Alpha Beta | 3-Layer(bba) Sandwich | FAD/NAD(P)-binding domain | FAD/NAD(P)-binding domain | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF00070 | Pyridine nucleotide-disulphide oxidoreductase (Pyr_redox) | Pyridine nucleotide-disulphide oxidoreductase | This 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 |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR005982 | Thioredoxin reductase | Family | |
IPR023753 | FAD/NAD(P)-binding domain | Domain | |
IPR036188 | FAD/NAD(P)-binding domain superfamily | Homologous Superfamily | |
IPR008255 | Pyridine nucleotide-disulphide oxidoreductase, class-II, active site | Active Site |
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage
Chains | Enzyme Name | Description | Catalytic Residues |
---|---|---|---|
Thioredoxin reductase M-CSA #381 | Thioredoxin reductase contains FAD and NADPH binding domains that are structurally similar to the corresponding domains of the related enzyme glutathione reductase. The relative orientation of these domains is, however, very different in the two enzymes: when the FAD domains of thioredoxin and glutathione reductases are superimposed, the NADPH domain of one is rotated by 66 degrees with respect to the other. The observed binding mode of NADP+ in thioredoxin reductase is non-productive in that the nicotinamide ring is more than 17 A from the flavin ring system. Thioredoxin reductase belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | EC: 1.6.4.5 (PDB Primary Data) |