MolNFT v1 · #33287 · protein
Crystal structure of human thioredoxin reductase 1
2CFY: “Crystal structure of human thioredoxin reductase 1”. X-ray diffraction, 1 ligand (FAD), 20 pockets (best druggability 0.84). MolNFT v1 #33287 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2CFY
- Type
- protein
- Length
- 2,904 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin reductase 1
- EC
- 1.8.1.9
- UniProt
- Q16881
- Ligands
- FAD
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Thioredoxin reductase 1 (EC 1.8.1.9) | protein | 484 | 33% helix, 26% strand | Q16881 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 818 | 0.84 | 0.87 | 93 | empty |
| 2 | 773 | 0.84 | 0.87 | 91 | empty |
| 3 | 803 | 0.84 | 0.86 | 89 | empty |
| 4 | 973 | 0.82 | 0.83 | 111 | FAD |
| 5 | 923 | 0.81 | 0.83 | 101 | FAD |
Interfaces
9 interfaces between chains.
- A–B · 3433 Ų buried · 28 hydrogen bonds · protein-protein
- C–D · 3406 Ų buried · 27 hydrogen bonds · protein-protein
- E–F · 3372 Ų buried · 25 hydrogen bonds · protein-protein
- B–C · 366 Ų buried · 2 hydrogen bonds · protein-protein
- D–E · 250 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2CFY · Crystal structure of human thioredoxin reductase 1 · 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 Q16881
- Elsewhere: RCSB PDB 2CFY · PDBe 2CFY · UniProt Q16881
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