MolNFT v1 · #176066 · protein
Vibrio cholera aldehyde-alcohol dehrogenase
7DAG · Aldehyde-alcohol dehydrogenase: “Vibrio cholera aldehyde-alcohol dehrogenase”. Electron microscopy, 20 pockets (best druggability 0.90). MolNFT v1 #176066 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7DAG
- Type
- protein
- Length
- 6,069 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aldehyde-alcohol dehydrogenase
- UniProt
- A0A0E4GKF5
- Pockets
- 20 · best druggability 0.90
Structure
electron microscopy · 3 distinct chains · 43% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Aldehyde-alcohol dehydrogenase | protein | 867 | 43% helix, 13% strand | A0A0E4GKF5 |
| G | Aldehyde-alcohol dehydrogenase | protein | 419 | 47% helix, 9% strand | A0A0E4GKF5 |
| H | Aldehyde-alcohol dehydrogenase | protein | 448 | 41% helix, 17% strand | A0A0E4GKF5 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1054 | 0.90 | 0.91 | 150 | empty |
| 2 | 1014 | 0.89 | 0.91 | 152 | empty |
| 3 | 777 | 0.89 | 0.92 | 141 | empty |
| 4 | 971 | 0.89 | 0.91 | 144 | empty |
| 5 | 1079 | 0.87 | 0.88 | 135 | empty |
Interfaces
10 interfaces between chains.
- C–D · 3375 Ų buried · 28 hydrogen bonds · protein-protein
- E–F · 3315 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 3297 Ų buried · 30 hydrogen bonds · protein-protein
- B–C · 1621 Ų buried · 5 hydrogen bonds · protein-protein
- D–E · 1487 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 7DAG · Vibrio cholera aldehyde-alcohol dehrogenase · 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 A0A0E4GKF5
- Elsewhere: RCSB PDB 7DAG · PDBe 7DAG · UniProt A0A0E4GKF5
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