Research workbench
Crystal structure of substrate-bound P450CIN
Analyse Crystal structure of substrate-bound P450CIN in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FMX
- Type
- protein
- Length
- 794 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- P450CIN
- UniProt
- Q8VQF6
- Ligands
- HEM, CNL, SO4
- Pockets
- 7 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | P450CIN | protein | 397 | 51% helix, 12% strand | Q8VQF6 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- CNL · 1,3,3-trimethyl-2-oxabicyclo[2.2.2]octane · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 430 | 0.86 | 0.94 | 50 | HEM, CNL |
| 2 | 420 | 0.86 | 0.93 | 46 | HEM, CNL |
| 3 | 830 | 0.72 | 0.77 | 77 | empty |
| 4 | 61 | 0.43 | 0.82 | 13 | empty |
| 5 | 68 | 0.43 | 0.81 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 265 Ų buried · 1 hydrogen bond · protein-protein
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 Q8VQF6
- Elsewhere: RCSB PDB 4FMX · PDBe 4FMX · UniProt Q8VQF6
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