Research workbench
Crystal structure of substrate-free P450CIN
Analyse Crystal structure of substrate-free P450CIN in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FB2
- Type
- protein
- Length
- 1,566 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- P450CIN
- UniProt
- Q8VQF6
- Ligands
- HEM, CL
- Pockets
- 14 · best druggability 0.83
Structure
x-ray diffraction · 3 distinct chains · 49% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | P450CIN | protein | 392 | 49% helix, 11% strand | Q8VQF6 |
| C | P450CIN | protein | 391 | 50% helix, 11% strand | Q8VQF6 |
| D | P450CIN | protein | 391 | 49% helix, 11% strand | Q8VQF6 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · 4 copies · chains A, B, C, D
- EDO · 1,2-ethanediol · additive · 5 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 860 | 0.83 | 0.85 | 75 | HEM, EDO |
| 2 | 929 | 0.83 | 0.84 | 80 | HEM |
| 3 | 867 | 0.82 | 0.84 | 70 | HEM |
| 4 | 867 | 0.82 | 0.84 | 79 | HEM |
| 5 | 233 | 0.70 | 0.86 | 46 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1028 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 283 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 212 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 58 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 41 Ų buried · 0 hydrogen bonds · 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 4FB2 · PDBe 4FB2 · UniProt Q8VQF6
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