PDB ID: pdb_00004bmm
- Crystal structure of Trypanosoma cruzi CYP51 bound to the inhibitor (R)-N-(3-(1H-indol-3-yl)-1-oxo-1-(pyridin-4-ylamino)propan-2-yl)-2',3, 5'-trifluoro-(1,1'-biphenyl)-4-carboxamide
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2.84 Å
- Deposition date: 2013-05-09
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 (TU1  TU1
), L (TU1TU1
)
|
Each chain information
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 30-477 (32-481) |
| Mutations (UniProt numbering) | |
| Missing residues | 252ALA-257ASN |
| Structural gaps | Exists |
| Uniprot ID | Q7Z1V1 ￫UniprotKB |
| label_asym_ids of heme | G |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.20 Å |
| auth_asym_id | D |
|---|---|
| Residue indices (Uniprot) | 30-477 (32-481) |
| Mutations (UniProt numbering) | |
| Missing residues | 253SER-258THR |
| Structural gaps | Exists |
| Uniprot ID | Q7Z1V1 ￫UniprotKB |
| label_asym_ids of heme | K |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.15 Å |
| Structural data | modeled |
|---|---|
| Oligomeric count | 2 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
F (TU1TU1
), J (TU1TU1
)
|
Each chain information
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 30-477 (32-481) |
| Mutations (UniProt numbering) | |
| Missing residues | 252ALA-258THR |
| Structural gaps | Exists |
| Uniprot ID | Q7Z1V1 ￫UniprotKB |
| label_asym_ids of heme | E |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.18 Å |
| auth_asym_id | C |
|---|---|
| Residue indices (Uniprot) | 30-477 (32-481) |
| Mutations (UniProt numbering) | |
| Missing residues | 252ALA-259SER |
| Structural gaps | Exists |
| Uniprot ID | Q7Z1V1 ￫UniprotKB |
| label_asym_ids of heme | I |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.18 Å |