Research workbench
Acinetobacter baumannii thioredoxin reductase
Analyse Acinetobacter baumannii thioredoxin reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E52
- Type
- protein
- Length
- 314 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin reductase
- EC
- 1.8.1.9
- UniProt
- A0A062FG66
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin reductase (EC 1.8.1.9) | protein | 314 | 29% helix, 30% strand | A0A062FG66 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 461 | 0.71 | 0.81 | 75 | empty |
| 2 | 130 | 0.43 | 0.76 | 22 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7E52 · Acinetobacter baumannii Thioredoxin reductase · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A0A062FG66
- Elsewhere: RCSB PDB 7E52 · PDBe 7E52 · UniProt A0A062FG66
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