Research workbench
Structure of alcohol dehydrogenase from drosophila lebanonesis T114V mutant complexed with NAD+
Analyse Structure of alcohol dehydrogenase from drosophila lebanonesis T114V mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RJ5
- Type
- protein
- Length
- 504 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alcohol dehydrogenase
- EC
- 1.1.1.1
- UniProt
- P10807
- Ligands
- NAD
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alcohol dehydrogenase (EC 1.1.1.1) | protein | 254 | 44% helix, 18% strand | P10807 |
| B | Alcohol dehydrogenase (EC 1.1.1.1) | protein | 250 | 44% helix, 18% strand | P10807 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 337 | 0.73 | 0.85 | 44 | ACY, NAD |
| 2 | 413 | 0.66 | 0.79 | 41 | empty |
| 3 | 235 | 0.62 | 0.81 | 49 | empty |
| 4 | 59 | 0.29 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 2590 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 3RJ5 · Structure of alcohol dehydrogenase from Drosophila leba sis T114V mutant complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- P10807 · AlphaFold monomer V2.0 prediction for alcohol dehydrogenase (P10807) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P10807
- Elsewhere: RCSB PDB 3RJ5 · PDBe 3RJ5 · UniProt P10807
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.