Research workbench
Cryo-EM structure of aldehyde-alcohol dehydrogenase reveals a high- order helical architecture critical for its activity
Analyse Cryo-EM structure of aldehyde-alcohol dehydrogenase reveals a high- order… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AHC
- Type
- protein
- Length
- 6,052 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aldehyde-alcohol dehydrogenase
- EC
- 1.1.1.1, 1.2.1.10
- UniProt
- P0A9Q7
- Pockets
- 20 · best druggability 0.89
Structure
electron microscopy · 2 distinct chains · 42% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, H | Aldehyde-alcohol dehydrogenase (EC 1.1.1.1, 1.2.1.10) | protein | 419 | 44% helix, 9% strand | P0A9Q7 |
| B, C, D, E, F, G | Aldehyde-alcohol dehydrogenase (EC 1.1.1.1, 1.2.1.10) | protein | 869 | 41% helix, 14% strand | P0A9Q7 |
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 | 1011 | 0.89 | 0.90 | 124 | empty |
| 2 | 937 | 0.88 | 0.90 | 116 | empty |
| 3 | 886 | 0.88 | 0.90 | 100 | empty |
| 4 | 828 | 0.87 | 0.90 | 109 | empty |
| 5 | 563 | 0.85 | 0.91 | 74 | empty |
Interfaces
9 interfaces between chains.
- F–G · 4042 Ų buried · 26 hydrogen bonds · protein-protein
- D–E · 4039 Ų buried · 26 hydrogen bonds · protein-protein
- B–C · 3951 Ų buried · 25 hydrogen bonds · protein-protein
- E–F · 2118 Ų buried · 19 hydrogen bonds · protein-protein
- C–D · 2086 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 6AHC · Cryo-EM structure of aldehyde-alcohol dehydrogenase reveals a high-order helical… · the same entry in another collection · chain H against H, TM-score 1.00
- P0A9Q7 · AlphaFold monomer V2.0 prediction for aldehyde-alcohol dehydrogenase (P0A9Q7) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P0A9Q7
- Elsewhere: RCSB PDB 6AHC · PDBe 6AHC · UniProt P0A9Q7
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