Research workbench
Human aldose reductase complexed with novel sulfonyl- pyridazinone inhibitor
Analyse Human aldose reductase complexed with novel sulfonyl- pyridazinone inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z89
- 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
- NAP, 62P
- Pockets
- 2 · best druggability 0.74
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
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- 62P · 6-[(5-chloro-3-methyl-1-benzofuran-2-yl)sulfonyl]pyridazin-3(2H)-one · 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 | 336 | 0.74 | 0.86 | 50 | NAP, 62P |
| 2 | 59 | 0.44 | 0.83 | 20 | empty |
Compared structures
- 1Z89 · Human Aldose Reductase complexed with novel Sulfonyl-pyridazi Inhibitor · 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 1Z89 · PDBe 1Z89
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