MolNFT v1 · #14483 · protein
Refined 1.8 ångströms structure of human aldose reductase complexed with the potent inhibitor zopolrestat
1MAR: “Refined 1.8 ångströms structure of human aldose reductase complexed with the potent inhibitor zopolrestat”. X-ray diffraction, 2 ligands (NAP, ZST). MolNFT v1 #14483 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1MAR
- Type
- protein
- Length
- 315 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
- NAP, ZST
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aldose reductase (EC 1.1.1.21) | protein | 315 | 0% helix, 0% strand | P15121 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- ZST · 3,4-dihydro-4-oxo-3-((5-trifluoromethyl-2-benzothiazolyl)methyl)-1-phthalazine acetic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1MAR · Refined 1.8 ångströms structure of human aldose reductase complexed with the potent… · 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 1MAR · PDBe 1MAR · UniProt P15121
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