Research workbench
P450CAM from pseudomonas putida reconstituted with manganic protoporphyrin IX
Analyse P450CAM from pseudomonas putida reconstituted with manganic protoporphyrin IX in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FE6
- 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
- MNR, K
- Pockets
- 2 · best druggability 0.87
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
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 545 | 0.87 | 0.92 | 51 | MNR |
| 2 | 57 | 0.32 | 0.77 | 15 | empty |
Compared structures
- 2FE6 · P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX · 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 1.00
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 2FE6 · PDBe 2FE6 · UniProt P00183
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.