Research workbench
Codeinone reductase isoform 1.3 apo form
Analyse Codeinone reductase isoform 1.3 apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MBF
- Type
- protein
- Length
- 1,843 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADPH-dependent codeinone reductase 1-3
- EC
- 1.1.1.247
- UniProt
- Q9SQ68
- Pockets
- 12 · best druggability 0.87
Structure
x-ray diffraction · 6 distinct chains · 40% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH-dependent codeinone reductase 1-3 (EC 1.1.1.247) | protein | 310 | 41% helix, 16% strand | Q9SQ68 |
| B | NADPH-dependent codeinone reductase 1-3 (EC 1.1.1.247) | protein | 310 | 41% helix, 17% strand | Q9SQ68 |
| C | NADPH-dependent codeinone reductase 1-3 (EC 1.1.1.247) | protein | 301 | 38% helix, 16% strand | Q9SQ68 |
| D | NADPH-dependent codeinone reductase 1-3 (EC 1.1.1.247) | protein | 309 | 43% helix, 16% strand | Q9SQ68 |
| E | NADPH-dependent codeinone reductase 1-3 (EC 1.1.1.247) | protein | 308 | 41% helix, 15% strand | Q9SQ68 |
| F | NADPH-dependent codeinone reductase 1-3 (EC 1.1.1.247) | protein | 305 | 38% helix, 17% strand | Q9SQ68 |
Pockets
12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1033 | 0.87 | 0.88 | 133 | empty |
| 2 | 1054 | 0.86 | 0.87 | 114 | empty |
| 3 | 1093 | 0.82 | 0.83 | 107 | empty |
| 4 | 138 | 0.65 | 0.87 | 29 | empty |
| 5 | 305 | 0.54 | 0.75 | 41 | empty |
Interfaces
5 interfaces between chains.
- A–D · 1208 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 1101 Ų buried · 15 hydrogen bonds · protein-protein
- E–F · 1021 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 614 Ų buried · 5 hydrogen bonds · protein-protein
- A–E · 194 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
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 Q9SQ68
- Elsewhere: RCSB PDB 7MBF · PDBe 7MBF · UniProt Q9SQ68
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