MolNFT v1 · #49887 · protein
Human aldose reductase structure
2R24: “Human aldose reductase structure”. X-ray diffraction; neutron diffraction, 2 ligands (NAP, LDT), 1 pocket (best druggability 0.74). MolNFT v1 #49887 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2R24
- Type
- protein
- Length
- 316 residues
- Chains
- 1
- Method
- x-ray diffraction; neutron diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aldose reductase
- EC
- 1.1.1.21
- UniProt
- P15121
- Ligands
- NAP, LDT
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction; neutron diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aldose reductase (EC 1.1.1.21) | protein | 316 | 40% helix, 15% strand | P15121 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- LDT · Idd594 · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 349 | 0.74 | 0.85 | 50 | NAP, LDT |
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 2R24 · PDBe 2R24 · UniProt P15121
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