MolNFT v1 · #81797 · protein
Aldose reductase complexed with glceraldehyde
3V36: “Aldose reductase complexed with glceraldehyde”. X-ray diffraction, 3 ligands (NAP, 3GR, 0PY), 3 pockets (best druggability 0.70). MolNFT v1 #81797 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3V36
- 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
- UniProt
- P15121
- Ligands
- NAP, 3GR, 0PY
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aldose reductase (EC 1.1.1.21) | protein | 316 | 38% helix, 15% strand | P15121 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- 3GR · D-Glyceraldehyde · ligand · chains A
- 0PY · pyridine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 332 | 0.70 | 0.83 | 49 | NAP, 3GR |
| 2 | 54 | 0.32 | 0.77 | 20 | empty |
| 3 | 53 | 0.28 | 0.75 | 13 | empty |
Compared structures
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 3V36 · PDBe 3V36 · UniProt P15121
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