MolNFT v1 · #103909 · protein
Human aldose reductase complexed with a ligand with an idd structure (2-[5-fluoro-2-(prop-2-YNYLCARBAMOYL)PHENOXY]ACETIC acid) at 1.12 a
4PUW: “Human aldose reductase complexed with a ligand with an idd structure…”. X-ray diffraction, 2 ligands (2WQ, NAP), 2 pockets (best druggability 0.68). MolNFT v1 #103909 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4PUW
- Type
- protein
- Length
- 316 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aldose reductase
- EC
- 1.1.1.21
- UniProt
- P15121
- Ligands
- 2WQ, NAP
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aldose reductase (EC 1.1.1.21) | protein | 316 | 38% helix, 15% strand | P15121 |
Ligands and binding sites
- 2WQ · [5-fluoro-2-(prop-2-yn-1-ylcarbamoyl)phenoxy]acetic acid · ligand · chains A
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- CIT · Citric acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 285 | 0.68 | 0.83 | 43 | 2WQ, NAP |
| 2 | 67 | 0.47 | 0.84 | 19 | empty |
Compared structures
- 4PUW · Human Aldose Reductase complexed with a ligand with an IDD structure… · the same entry in another collection · chain A against A, TM-score 1.00
- P15121 · AlphaFold monomer V2.0 prediction for aldo-keto reductase family 1 member B1 (P15121) · a predicted model of the same protein · 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 P15121
- Elsewhere: RCSB PDB 4PUW · PDBe 4PUW · UniProt P15121
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