Research workbench
Porcine aldehyde reductase in ternary complex with inhibitor
Analyse Porcine aldehyde reductase in ternary complex with inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FX4
- Type
- protein
- Length
- 325 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alcohol dehydrogenase [NADP+]
- EC
- 1.1.1.2
- UniProt
- P50578
- Ligands
- NAP, FX4, SO4
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alcohol dehydrogenase [NADP+] (EC 1.1.1.2) | protein | 325 | 37% helix, 18% strand | P50578 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- FX4 · [(5Z)-5-{[3-(carboxymethoxy)-4-methoxyphenyl]methylidene}-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid · ligand · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 510 | 0.72 | 0.81 | 51 | NAP, FX4 |
| 2 | 57 | 0.47 | 0.85 | 20 | empty |
| 3 | 92 | 0.35 | 0.74 | 23 | empty |
| 4 | 59 | 0.29 | 0.74 | 14 | empty |
Compared structures
- 3FX4 · Porcine aldehyde reductase in ternary complex with inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
- P50578 · AlphaFold monomer V2.0 prediction for aldo-keto reductase family 1 member A1 (P50578) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P50578
- Elsewhere: RCSB PDB 3FX4 · PDBe 3FX4 · UniProt P50578
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.