Research workbench
Human aldose reductase in complex with NADP+ in space group P212121
Analyse Human aldose reductase in complex with NADP+ in space group P212121 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3Q65
- 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, SO4
- Pockets
- 5 · best druggability 0.85
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
- SO4 · Sulfate ion · ion · 9 copies · chains A, B
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1107 | 0.85 | 0.85 | 134 | NAP |
| 2 | 75 | 0.42 | 0.80 | 19 | empty |
| 3 | 65 | 0.32 | 0.75 | 20 | GOL |
| 4 | 60 | 0.30 | 0.75 | 11 | empty |
| 5 | 55 | 0.30 | 0.75 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 681 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 3Q65 · Human Aldose Reductase in Complex with NADP+ in Space Group P212121 · 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 3Q65 · PDBe 3Q65 · UniProt P15121
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