MolNFT v1 · #33605 · protein
High-resolution crystal structure of cytochrome P450-cam
2CPP: “High-resolution crystal structure of cytochrome P450-cam”. X-ray diffraction, 2 ligands (HEM, CAM), 3 pockets (best druggability 0.86). MolNFT v1 #33605 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2CPP
- 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, CAM
- Pockets
- 3 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450-cam (EC 1.14.15.1) | protein | 405 | 52% helix, 11% strand | P00183 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 453 | 0.86 | 0.93 | 49 | HEM, CAM |
| 2 | 85 | 0.43 | 0.80 | 16 | empty |
| 3 | 50 | 0.31 | 0.76 | 14 | 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 2CPP · PDBe 2CPP · UniProt P00183
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