Research workbench
Inhibitor-induced conformational change in cytochrome P450-cam
Analyse Inhibitor-induced conformational change in cytochrome P450-cam in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PHB
- Type
- protein
- Length
- 405 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450-cam
- EC
- 1.14.15.1
- UniProt
- P00183
- Ligands
- HEM, PFZ
- Pockets
- 2 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450-cam (EC 1.14.15.1) | protein | 405 | 52% helix, 10% strand | P00183 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- PFZ · 1-(N-imidazolyl)-2-hydroxy-2-(2,3-dichlorophenyl)octane · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 501 | 0.86 | 0.92 | 55 | HEM, PFZ |
| 2 | 66 | 0.41 | 0.81 | 13 | empty |
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 P00183
- Elsewhere: RCSB PDB 1PHB · PDBe 1PHB · UniProt P00183
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