MolNFT v1 · #43295 · protein
Reduced and co-bound cytochrome P450CAM (CYP101A1)
2L8M · Camphor 5-monooxygenase: “Reduced and co-bound cytochrome P450CAM (CYP101A1)”. Solution nmr, 5 ligands (CAM, HEM, K), 4 pockets (best druggability 0.86). MolNFT v1 #43295 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2L8M
- 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
- CAM, HEM, K, CL, CMO
- Pockets
- 4 · best druggability 0.86
Structure
solution nmr · 1 distinct chain · 48% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Camphor 5-monooxygenase (EC 1.14.15.1) | protein | 405 | 48% helix, 10% strand | P00183 |
Ligands and binding sites
- CAM · Camphor · ligand · chains A
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- K · Potassium ion · metal · 4 copies · chains A
- CL · Chloride ion · ion · 3 copies
- CMO · Carbon monoxide · ion · 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 | 551 | 0.86 | 0.92 | 56 | CAM, HEM, CMO |
| 2 | 103 | 0.42 | 0.78 | 15 | empty |
| 3 | 88 | 0.40 | 0.77 | 17 | empty |
| 4 | 71 | 0.31 | 0.74 | 21 | 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 2L8M · PDBe 2L8M · UniProt P00183
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.