MolNFT v1 · #67708 · protein
Crystal structure of helicobacter pylori thioredoxin reductase
3ISH: “Crystal structure of helicobacter pylori thioredoxin reductase”. X-ray diffraction, 1 ligand (FAD), 6 pockets (best druggability 0.83). MolNFT v1 #67708 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3ISH
- Type
- protein
- Length
- 933 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin reductase
- UniProt
- P56431
- Ligands
- FAD
- Pockets
- 6 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Thioredoxin reductase | protein | 311 | 27% helix, 32% strand | P56431 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 724 | 0.83 | 0.87 | 108 | FAD |
| 2 | 456 | 0.80 | 0.88 | 58 | FAD |
| 3 | 1156 | 0.78 | 0.80 | 120 | FAD |
| 4 | 54 | 0.68 | 0.97 | 19 | empty |
| 5 | 106 | 0.56 | 0.84 | 19 | empty |
Interfaces
2 interfaces between chains.
- A–B · 2278 Ų buried · 29 hydrogen bonds · protein-protein
- B–C · 1128 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
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 P56431
- Elsewhere: RCSB PDB 3ISH · PDBe 3ISH · UniProt P56431
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