Research workbench
Covalent attachment of an electroactive sulphydryl reagent in the active site of cytochrome P450CAM
Analyse Covalent attachment of an electroactive sulphydryl reagent in the active site… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GJM
- 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
- FEM, HEM
- Pockets
- 3 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450-cam (EC 1.14.15.1) | protein | 405 | 50% helix, 13% strand | P00183 |
Ligands and binding sites
- FEM · N-(2-ferrocenylethyl)maleimide · ligand · 2 copies · chains A
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
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 | 511 | 0.88 | 0.94 | 59 | HEM, FEM |
| 2 | 94 | 0.37 | 0.76 | 18 | empty |
| 3 | 67 | 0.33 | 0.76 | 18 | empty |
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 1GJM · Covalent attachment of an electroactive sulphydryl reagent in the active site of… · the same entry in another collection · chain A against A, TM-score 1.00
- P00183 · AlphaFold monomer V2.0 prediction for camphor 5-monooxygenase (P00183) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 1GJM · PDBe 1GJM · UniProt P00183
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