PDB ID: pdb_00006dwm
- Structure of Human Cytochrome P450 1A1 with Bergamottin
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2.85 Å
- Deposition date: 2018-06-26
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 (HJJ  HJJ
), G (CPS CPS
)
|
Each chain information
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 35-512 (35-512) |
| Mutations (UniProt numbering) | |
| Missing residues | 293GLN-300VAL |
| Structural gaps | Exists |
| Uniprot ID | P04798 ￫UniprotKB |
| label_asym_ids of heme | E |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.10 Å |
| Structural data | PDB |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
I (HJJHJJ
), J (GOL GOL
)
|
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
L (HJJHJJ
)
|
Each chain information
| auth_asym_id | C |
|---|---|
| Residue indices (Uniprot) | 38-512 (35-512) |
| Mutations (UniProt numbering) | |
| Missing residues | 292LYS-302LEU |
| Structural gaps | Exists |
| Uniprot ID | P04798 ￫UniprotKB |
| label_asym_ids of heme | K |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.12 Å |
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
N (HJJHJJ
), O (CPSCPS
), P (GOLGOL
)
|
Each chain information
| auth_asym_id | D |
|---|---|
| Residue indices (Uniprot) | 39-512 (35-512) |
| Mutations (UniProt numbering) | |
| Missing residues | 292LYS-301GLN |
| Structural gaps | Exists |
| Uniprot ID | P04798 ￫UniprotKB |
| label_asym_ids of heme | M |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.11 Å |