MolNFT v1 · #37377 · protein
Human aldose reductase complexed with tolrestat at 1.08 a resolution.
2FZD: “Human aldose reductase complexed with tolrestat at 1.08 a resolution.”. X-ray diffraction, 2 ligands (NAP, TOL), 2 pockets (best druggability 0.72). MolNFT v1 #37377 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2FZD
- Type
- protein
- Length
- 313 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aldose reductase
- EC
- 1.1.1.21
- UniProt
- Q5U031
- Ligands
- NAP, TOL
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aldose reductase (EC 1.1.1.21) | protein | 313 | 40% helix, 15% strand | Q5U031 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- TOL · Tolrestat · ligand · 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 | 309 | 0.72 | 0.85 | 48 | NAP, TOL |
| 2 | 57 | 0.32 | 0.76 | 17 | empty |
Compared structures
- 2FZD · Human aldose reductase complexed with tolrestat at 1.08 A resolution. · the same entry in another collection · 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 Q5U031
- Elsewhere: RCSB PDB 2FZD · PDBe 2FZD · UniProt Q5U031
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