MolNFT v1 · #29279 · protein
Human aldose reductase in complex with NADP+ and the inhibitor lidorestat at 1.04 ångström
1Z3N: “Human aldose reductase in complex with NADP+ and the inhibitor lidorestat at 1.04 ångström”. X-ray diffraction, 2 ligands (NDP, 3NA), 1 pocket (best druggability 0.75). MolNFT v1 #29279 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1Z3N
- 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
- Ligands
- NDP, 3NA
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aldose reductase (EC 1.1.1.21) | protein | 316 | 39% helix, 15% strand | — |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- 3NA · {3-[(4,5,7-trifluoro-1,3-benzothiazol-2-yl)methyl]-1H-indol-1-yl}acetic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 313 | 0.75 | 0.86 | 45 | NDP, 3NA |
Compared structures
- 1Z3N · Human aldose reductase in complex with NADP+ and the inhibitor lidorestat at 1.04 angstrom · 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
- Elsewhere: RCSB PDB 1Z3N · PDBe 1Z3N
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