MolNFT v1 · #129779 · protein
Crystal structure of human AKR1B1 complexed with NADP+ and compound 41
5OUK: “Crystal structure of human AKR1B1 complexed with NADP+ and compound 41”. X-ray diffraction, 2 ligands (NAP, AVT). MolNFT v1 #129779 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5OUK
- Type
- protein
- Length
- 316 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P15121
- Ligands
- NAP, AVT
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 316 | — | P15121 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- AVT · 2-[9-fluoranyl-5-(4-methoxyphenyl)-3-methyl-1-oxidanylidene-pyrimido[4,5-c]quinolin-2-yl]ethanoic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OUK · Crystal structure of human AKR1B1 complexed with NADP+ and compound 41 · 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 0.99
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 5OUK · PDBe 5OUK · UniProt P15121
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