PDB ID: pdb_00005wbg
- Crystal Structure of human Cytochrome P450 2B6 (Y226H/K262R) in complex with an analog of a drug Efavirenz
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2.99 Å
- Deposition date: 2017-06-29
Number of assemblies: 6
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
H (9ZJ |
Each chain information
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 28-491 (21-491) |
| Mutations (UniProt numbering) | |
| Missing residues | 278ASN-278ASN |
| Structural gaps | Exists |
| Uniprot ID | P20813 →UniprotKB |
| label_asym_ids of heme | G |
| 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 |
K (9ZJ |
Each chain information
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 27-491 (21-491) |
| Mutations (UniProt numbering) | |
| Missing residues | 278ASN-278ASN |
| Structural gaps | Exists |
| Uniprot ID | P20813 →UniprotKB |
| label_asym_ids of heme | J |
| 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 (9ZJ |
Each chain information
| auth_asym_id | C |
|---|---|
| Residue indices (Uniprot) | 27-491 (21-491) |
| Mutations (UniProt numbering) | |
| Missing residues | 278ASN-278ASN |
| Structural gaps | Exists |
| Uniprot ID | P20813 →UniprotKB |
| label_asym_ids of heme | M |
| 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 |
Q (9ZJ |
Each chain information
| auth_asym_id | D |
|---|---|
| Residue indices (Uniprot) | 27-491 (21-491) |
| Mutations (UniProt numbering) | |
| Missing residues | 278ASN-278ASN |
| Structural gaps | Exists |
| Uniprot ID | P20813 →UniprotKB |
| label_asym_ids of heme | P |
| 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 |
T (9ZJ |
Each chain information
| auth_asym_id | E |
|---|---|
| Residue indices (Uniprot) | 28-491 (21-491) |
| Mutations (UniProt numbering) | |
| Missing residues | 278ASN-278ASN |
| Structural gaps | Exists |
| Uniprot ID | P20813 →UniprotKB |
| label_asym_ids of heme | S |
| 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 |
W (CM5 |
Each chain information
| auth_asym_id | F |
|---|---|
| Residue indices (Uniprot) | 27-491 (21-491) |
| Mutations (UniProt numbering) | |
| Missing residues | 278ASN-278ASN |
| Structural gaps | Exists |
| Uniprot ID | P20813 →UniprotKB |
| label_asym_ids of heme | V |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.16 Å |

