PDB ID: pdb_00002x2n
- X-ray structure of cyp51 from trypanosoma brucei in complex with posaconazole in two different conformations
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2.6 Å
- Deposition date: 2010-01-14
Number of assemblies: 2
| Structural data | modeled |
|---|---|
| Oligomeric count | 2 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
H (X2N  X2N
), L (X2NX2N
)
|
Each chain information
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 30-477 (22-481) |
| Mutations (UniProt numbering) | |
| Missing residues | 253ASN-256SER |
| Structural gaps | Exists |
| Uniprot ID | Q385E8 ￫UniprotKB |
| label_asym_ids of heme | G |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.10 Å |
| auth_asym_id | D |
|---|---|
| Residue indices (Uniprot) | 30-477 (22-481) |
| Mutations (UniProt numbering) | |
| Missing residues | 255ASP-255ASP |
| Structural gaps | Exists |
| Uniprot ID | Q385E8 ￫UniprotKB |
| label_asym_ids of heme | K |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| Structural data | modeled |
|---|---|
| Oligomeric count | 2 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
F (X2NX2N
), J (X2NX2N
)
|
Each chain information
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 30-478 (22-481) |
| Mutations (UniProt numbering) | |
| Missing residues | 255ASP-255ASP |
| Structural gaps | Exists |
| Uniprot ID | Q385E8 ￫UniprotKB |
| label_asym_ids of heme | E |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.11 Å |
| auth_asym_id | C |
|---|---|
| Residue indices (Uniprot) | 30-477 (22-481) |
| Mutations (UniProt numbering) | |
| Missing residues | 251ALA-257SER |
| Structural gaps | Exists |
| Uniprot ID | Q385E8 ￫UniprotKB |
| label_asym_ids of heme | I |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |