MolNFT v1 · #110524 · protein
Crystal structure of human aldose reductase complexed with NADP+ and JF0048
4XZH: “Crystal structure of human aldose reductase complexed with NADP+ and JF0048”. X-ray diffraction, 2 ligands (NAP, 48I), 5 pockets (best druggability 0.83). MolNFT v1 #110524 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 4XZH
- Type
- protein
- Length
- 632 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aldose reductase
- EC
- 1.1.1.21
- UniProt
- P15121
- Ligands
- NAP, 48I
- Pockets
- 5 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aldose reductase (EC 1.1.1.21) | protein | 316 | 39% helix, 15% strand | P15121 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- 48I · [3-(4-chloro-3-nitrobenzyl)-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl]acetic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 949 | 0.83 | 0.84 | 109 | NAP, 48I |
| 2 | 307 | 0.75 | 0.86 | 50 | NAP, 48I |
| 3 | 78 | 0.46 | 0.82 | 21 | empty |
| 4 | 154 | 0.46 | 0.76 | 21 | empty |
| 5 | 66 | 0.43 | 0.82 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 762 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 4XZH · Crystal structure of human Aldose Reductase complexed with NADP+ and JF0048 · 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 4XZH · PDBe 4XZH · UniProt P15121
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.