Research workbench
Reduced and co-bound cytochrome P450CAM (CYP101A1)
Analyse Reduced and co-bound cytochrome P450CAM (CYP101A1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LQD
- Type
- protein
- Length
- 405 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Camphor 5-monooxygenase
- EC
- 1.14.15.1
- UniProt
- P00183
- Ligands
- HEM, K, CMO
- Pockets
- 5 · best druggability 0.87
Structure
solution nmr · 1 distinct chain · 46% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Camphor 5-monooxygenase (EC 1.14.15.1) | protein | 405 | 46% helix, 13% strand | P00183 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- K · Potassium ion · metal · chains A
- CMO · Carbon monoxide · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 487 | 0.87 | 0.94 | 49 | HEM, CMO |
| 2 | 131 | 0.43 | 0.76 | 21 | empty |
| 3 | 58 | 0.42 | 0.82 | 20 | empty |
| 4 | 74 | 0.40 | 0.79 | 15 | empty |
| 5 | 66 | 0.39 | 0.79 | 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 2LQD · PDBe 2LQD · UniProt P00183
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