PDB ID: pdb_00003g5n
- Triple ligand occupancy crystal structure of cytochrome P450 2B4 in complex with the inhibitor 1-biphenyl-4-methyl-1H-imidazole
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2.5 Å
- Deposition date: 2009-02-05
Number of assemblies: 4
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
F (PB2 |
Each chain information
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 27-493 (20-491) |
| Mutations (UniProt numbering) | |
| Missing residues | 135PHE-138GLY:276LYS-282GLU |
| Structural gaps | Exists |
| Uniprot ID | P00178 →UniprotKB |
| label_asym_ids of heme | E |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.17 Å |
Each chain information
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 28-492 (20-491) |
| Mutations (UniProt numbering) | |
| Missing residues | 135PHE-138GLY:274LYS-283PHE |
| Structural gaps | Exists |
| Uniprot ID | P00178 →UniprotKB |
| label_asym_ids of heme | K |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.17 Å |
Each chain information
| auth_asym_id | C |
|---|---|
| Residue indices (Uniprot) | 26-492 (20-491) |
| Mutations (UniProt numbering) | |
| Missing residues | 135PHE-138GLY:274LYS-284HIS |
| Structural gaps | Exists |
| Uniprot ID | P00178 →UniprotKB |
| label_asym_ids of heme | O |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.19 Å |
Each chain information
| auth_asym_id | D |
|---|---|
| Residue indices (Uniprot) | 28-492 (20-491) |
| Mutations (UniProt numbering) | |
| Missing residues | 136GLY-139LYS:274LYS-283PHE |
| Structural gaps | Exists |
| Uniprot ID | P00178 →UniprotKB |
| label_asym_ids of heme | U |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.19 Å |

