PDB ID: pdb_00006vlt
- Crystal Structure of Human P450 2C9*2 Genetic Variant in Complex with Losartan
- Experimental method: X-RAY DIFFRACTION
- Resolution: 3.12 Å
- Deposition date: 2020-01-25
Number of assemblies: 8
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
J (LSN |
Each chain information
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 28-490 (19-490) |
| Mutations (UniProt numbering) | |
| Missing residues | 137GLY-138LYS |
| Structural gaps | Exists |
| Uniprot ID | P11712 →UniprotKB |
| label_asym_ids of heme | I |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.15 Å |
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
L (LSN |
Each chain information
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 28-491 (19-490) |
| Mutations (UniProt numbering) | |
| Missing residues | 135GLY-137GLY |
| Structural gaps | Exists |
| Uniprot ID | P11712 →UniprotKB |
| label_asym_ids of heme | K |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.16 Å |
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
N (LSN |
Each chain information
| auth_asym_id | C |
|---|---|
| Residue indices (Uniprot) | 28-491 (19-490) |
| Mutations (UniProt numbering) | |
| Missing residues | 135GLY-138LYS |
| Structural gaps | Exists |
| Uniprot ID | P11712 →UniprotKB |
| label_asym_ids of heme | M |
| 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 |
P (LSN |
Each chain information
| auth_asym_id | D |
|---|---|
| Residue indices (Uniprot) | 28-491 (19-490) |
| Mutations (UniProt numbering) | |
| Missing residues | 136MET-138LYS |
| Structural gaps | Exists |
| Uniprot ID | P11712 →UniprotKB |
| label_asym_ids of heme | O |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.16 Å |
Each chain information
| auth_asym_id | E |
|---|---|
| Residue indices (Uniprot) | 28-491 (19-490) |
| Mutations (UniProt numbering) | |
| Missing residues | 135GLY-138LYS |
| Structural gaps | Exists |
| Uniprot ID | P11712 →UniprotKB |
| label_asym_ids of heme | R |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.14 Å |
Each chain information
| auth_asym_id | F |
|---|---|
| Residue indices (Uniprot) | 28-491 (19-490) |
| Mutations (UniProt numbering) | |
| Missing residues | 135GLY-138LYS |
| Structural gaps | Exists |
| Uniprot ID | P11712 →UniprotKB |
| label_asym_ids of heme | W |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.15 Å |
Each chain information
| auth_asym_id | G |
|---|---|
| Residue indices (Uniprot) | 28-490 (19-490) |
| Mutations (UniProt numbering) | |
| Missing residues | 135GLY-135GLY |
| Structural gaps | Exists |
| Uniprot ID | P11712 →UniprotKB |
| label_asym_ids of heme | BA |
| 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) | 28-490 (19-490) |
| Mutations (UniProt numbering) | |
| Missing residues | 135GLY-138LYS |
| Structural gaps | Exists |
| Uniprot ID | P11712 →UniprotKB |
| label_asym_ids of heme | GA |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.14 Å |

