Research workbench
L244A mutant of cytochrome P450CAM complexed with imidazole
Analyse L244A mutant of cytochrome P450CAM complexed with imidazole in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2H7R
- 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, 1MZ
- Pockets
- 4 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450-cam (EC 1.14.15.1) | protein | 405 | 50% helix, 11% strand | P00183 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- 1MZ · 1-methylimidazole · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 391 | 0.86 | 0.94 | 47 | HEM, 1MZ |
| 2 | 76 | 0.37 | 0.78 | 17 | empty |
| 3 | 71 | 0.33 | 0.76 | 18 | empty |
| 4 | 50 | 0.27 | 0.75 | 17 | 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 2H7R · PDBe 2H7R · UniProt P00183
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