Research workbench
High resolution structure of mouse aldehyde reductase (AKR1A4) in its apo-form
Analyse High resolution structure of mouse aldehyde reductase (AKR1A4) in its apo-form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GAC
- Type
- protein
- Length
- 629 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alcohol dehydrogenase [NADP(+)]
- EC
- 1.1.1.2
- UniProt
- Q9JII6
- Pockets
- 6 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alcohol dehydrogenase [NADP(+)] (EC 1.1.1.2) | protein | 324 | 39% helix, 18% strand | Q9JII6 |
| B | Alcohol dehydrogenase [NADP(+)] (EC 1.1.1.2) | protein | 305 | 38% helix, 16% strand | Q9JII6 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
- FLC · Citrate anion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 455 | 0.70 | 0.80 | 59 | EDO, FLC |
| 2 | 426 | 0.69 | 0.81 | 95 | empty |
| 3 | 240 | 0.55 | 0.77 | 25 | empty |
| 4 | 106 | 0.44 | 0.78 | 18 | empty |
| 5 | 71 | 0.40 | 0.79 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 692 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 4GAC · High resolution structure of mouse aldehyde reductase (AKR1a4) in its apo-form · the same entry in another collection · chain A against A, TM-score 1.00
- Q9JII6 · AlphaFold monomer V2.0 prediction for aldo-keto reductase family 1 member A1 (Q9JII6) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q9JII6
- Elsewhere: RCSB PDB 4GAC · PDBe 4GAC · UniProt Q9JII6
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