MolNFT v1 · #111866 · protein
Human carbonyl reductase 1 with glutathione in a protective configuration
4Z3D · Carbonyl reductase [NADPH] 1: “Human carbonyl reductase 1 with glutathione in a protective configuration”. X-ray diffraction, 2 ligands (GSH, NDP), 13 pockets (best druggability 0.77). MolNFT v1 #111866 on GenesisL1: 3D structure…
- PDB
- 4Z3D
- Type
- protein
- Length
- 1,099 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonyl reductase [NADPH] 1
- EC
- 1.1.1.184, 1.1.1.197, 1.1.1.189
- UniProt
- P16152
- Ligands
- GSH, NDP
- Pockets
- 13 · best druggability 0.77
Structure
x-ray diffraction · 3 distinct chains · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonyl reductase [NADPH] 1 (EC 1.1.1.184, 1.1.1.197, 1.1.1.189) | protein | 276 | 47% helix, 16% strand | P16152 |
| B | Carbonyl reductase [NADPH] 1 (EC 1.1.1.184, 1.1.1.197, 1.1.1.189) | protein | 275 | 48% helix, 16% strand | P16152 |
| C, D | Carbonyl reductase [NADPH] 1 (EC 1.1.1.184, 1.1.1.197, 1.1.1.189) | protein | 274 | 48% helix, 16% strand | P16152 |
Ligands and binding sites
- GSH · Glutathione · ligand · 4 copies · chains A, B, C, D
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1009 | 0.77 | 0.79 | 86 | GSH, NDP |
| 2 | 1020 | 0.76 | 0.79 | 86 | GSH, NDP |
| 3 | 415 | 0.72 | 0.83 | 47 | GSH, NDP |
| 4 | 456 | 0.70 | 0.81 | 53 | GSH, NDP |
| 5 | 265 | 0.65 | 0.82 | 33 | empty |
Interfaces
3 interfaces between chains.
- A–B · 635 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 629 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 537 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 4Z3D · Human carbonyl reductase 1 with glutathione in a protective configuration · the same entry in another collection · chain D against D, TM-score 1.00
- P16152 · AlphaFold monomer V2.0 prediction for carbonyl reductase [NADPH] 1 (P16152) · a predicted model of the same protein · chain D 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 4Z3D · PDBe 4Z3D · UniProt P16152
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