PDB ID: pdb_00008gk3
- Cytochrome P450 3A7 in complex with Dehydroepiandrosterone sulfate
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2.6 Å
- Deposition date: 2023-03-16
Number of assemblies: 12
| Structural data | PDB |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
N (ZWY |
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
Q (ZWY |
Each chain information
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 25-497 (24-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 263GLU-268ARG:281SER-285GLU |
| Structural gaps | Exists |
| Uniprot ID | P24462 →UniprotKB |
| label_asym_ids of heme | P |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.14 Å |
Each chain information
| auth_asym_id | C |
|---|---|
| Residue indices (Uniprot) | 29-497 (24-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 263GLU-268ARG |
| Structural gaps | Exists |
| Uniprot ID | P24462 →UniprotKB |
| label_asym_ids of heme | S |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
Each chain information
| auth_asym_id | D |
|---|---|
| Residue indices (Uniprot) | 28-497 (24-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 263GLU-268ARG:281SER-285GLU |
| Structural gaps | Exists |
| Uniprot ID | P24462 →UniprotKB |
| label_asym_ids of heme | X |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.14 Å |
Each chain information
| auth_asym_id | E |
|---|---|
| Residue indices (Uniprot) | 29-497 (24-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 263GLU-268ARG:282LYS-284SER |
| Structural gaps | Exists |
| Uniprot ID | P24462 →UniprotKB |
| label_asym_ids of heme | DA |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
Each chain information
| auth_asym_id | F |
|---|---|
| Residue indices (Uniprot) | 25-496 (24-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 263GLU-268ARG:281SER-285GLU |
| Structural gaps | Exists |
| Uniprot ID | P24462 →UniprotKB |
| label_asym_ids of heme | IA |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
Each chain information
| auth_asym_id | G |
|---|---|
| Residue indices (Uniprot) | 25-497 (24-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 263GLU-268ARG:281SER-285GLU |
| Structural gaps | Exists |
| Uniprot ID | P24462 →UniprotKB |
| label_asym_ids of heme | JA |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.15 Å |
Each chain information
| auth_asym_id | H |
|---|---|
| Residue indices (Uniprot) | 29-497 (24-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 263GLU-268ARG:281SER-285GLU |
| Structural gaps | Exists |
| Uniprot ID | P24462 →UniprotKB |
| label_asym_ids of heme | KA |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.14 Å |
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
PA (ZWY |
Each chain information
| auth_asym_id | I |
|---|---|
| Residue indices (Uniprot) | 29-497 (24-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 263GLU-268ARG |
| Structural gaps | Exists |
| Uniprot ID | P24462 →UniprotKB |
| label_asym_ids of heme | OA |
| 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 |
SA (ZWY |
Each chain information
| auth_asym_id | J |
|---|---|
| Residue indices (Uniprot) | 29-497 (24-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 263GLU-268ARG:282LYS-286THR |
| Structural gaps | Exists |
| Uniprot ID | P24462 →UniprotKB |
| label_asym_ids of heme | RA |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
Each chain information
| auth_asym_id | K |
|---|---|
| Residue indices (Uniprot) | 25-497 (24-503) |
| Mutations (UniProt numbering) | |
| Missing residues | 263GLU-268ARG:281SER-285GLU |
| Structural gaps | Exists |
| Uniprot ID | P24462 →UniprotKB |
| label_asym_ids of heme | UA |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.14 Å |

