MolNFT v2 · #209677 · protein
Crystal Structure Of Aldose Reductase (AKR1B1) Complexed With NADP+ And AT-003
8FH7: “Crystal Structure Of Aldose Reductase (AKR1B1) Complexed With NADP+ And AT-003”. X-ray diffraction at 1.45, 2 ligands (NAP, XY0). MolNFT v2 #209677 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 8FH7
- Type
- protein
- Length
- 315 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.45
- Source
- Homo sapiens
- UniProt
- P15121
- Ligands
- NAP, XY0
Structure
x-ray diffraction · resolution 1.45 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 315 | — | P15121 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- XY0 · {7-[(5-chloro-1,3-benzothiazol-2-yl)methyl]-8-oxo-7,8-dihydropyrazino[2,3-d]pyridazin-5-yl}acetic acid · ligand · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 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 8FH7 · PDBe 8FH7 · UniProt P15121
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