Research workbench
Crystal structure of human carbonyl reductase 1 in complex with glutathione
Analyse Crystal structure of human carbonyl reductase 1 in complex with glutathione in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BHJ
- Type
- protein
- Length
- 275 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonyl reductase [NADPH] 1
- EC
- 1.1.1.184
- UniProt
- P16152
- Ligands
- AB3, NAP, GSH, SO4
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonyl reductase [NADPH] 1 (EC 1.1.1.184) | protein | 275 | 49% helix, 16% strand | P16152 |
Ligands and binding sites
- AB3 · 3-(4-amino-1-tert-butyl-1H-pyrazolo[3,4-d]pyrimidin-3-yl)phenol · ligand · 2 copies · chains A
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- GSH · Glutathione · ligand · chains A
- SO4 · Sulfate ion · ion · 6 copies · chains A
- P33 · 3,6,9,12,15,18-hexaoxaicosane-1,20-diol · additive · 2 copies · chains A
- GOL · Glycerol · additive · 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 | 456 | 0.69 | 0.80 | 50 | AB3, NAP, GSH |
| 2 | 84 | 0.35 | 0.75 | 15 | empty |
| 3 | 67 | 0.31 | 0.75 | 12 | P33 |
Compared structures
- 3BHJ · Crystal structure of human Carbonyl Reductase 1 in complex with glutathione · the same entry in another collection · chain A against A, TM-score 1.00
- P16152 · AlphaFold monomer V2.0 prediction for carbonyl reductase [NADPH] 1 (P16152) · 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 P16152
- Elsewhere: RCSB PDB 3BHJ · PDBe 3BHJ · UniProt P16152
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.