PDB ID: pdb_00006wr0
- Human steroidogenic cytochrome P450 17A1 with 3-keto-delta4-abiraterone analog
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2.7 Å
- Deposition date: 2020-04-29
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 (U7P  U7P
)
|
Each chain information
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 31-504 (24-508) |
| Mutations (UniProt numbering) | |
| Missing residues | 275ASN-282GLN |
| Structural gaps | Exists |
| Uniprot ID | P05093 ￫UniprotKB |
| label_asym_ids of heme | E |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.11 Å |
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
H (U7PU7P
), I (CL CL
)
|
Each chain information
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 31-503 (24-508) |
| Mutations (UniProt numbering) | |
| Missing residues | 275ASN-282GLN |
| Structural gaps | Exists |
| Uniprot ID | P05093 ￫UniprotKB |
| label_asym_ids of heme | G |
| 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 |
K (U7PU7P
), L (CLCL
)
|
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
N (U7PU7P
), O (CLCL
)
|
Each chain information
| auth_asym_id | D |
|---|---|
| Residue indices (Uniprot) | 31-503 (24-508) |
| Mutations (UniProt numbering) | |
| Missing residues | 275ASN-281ASP |
| Structural gaps | Exists |
| Uniprot ID | P05093 ￫UniprotKB |
| label_asym_ids of heme | M |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |