PDB ID:  pdb_00004bjk
  • CYP51 of Trypanosoma brucei bound to (S)-N-(3-(1H-indol-3-yl)-1-oxo-1- (pyridin-4-ylamino)propan-2-yl)-3,3'-difluoro-(1,1'-biphenyl)-4- carboxamide
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 2.67 Å
  • Deposition date: 2013-04-18
Number of assemblies:  4
Assembly ID:  1  (author_and_software_defined_assembly)    
Structural data PDB
Oligomeric count 1
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others F (18IStructure of 18I18I )
Each chain information
Chain A heme  
auth_asym_id A
Residue indices (Uniprot) 29-478 (32-481)
Mutations (UniProt numbering)
Uniprot ID Q385E8 →UniprotKB
label_asym_ids of heme E
Available structure PDB
Assembly ID:  2  (author_and_software_defined_assembly)    
Structural data PDB
Oligomeric count 1
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others H (18IStructure of 18I18I )
Each chain information
Chain B heme  
auth_asym_id B
Residue indices (Uniprot) 29-478 (32-481)
Mutations (UniProt numbering)
Uniprot ID Q385E8 →UniprotKB
label_asym_ids of heme G
Available structure PDB
Assembly ID:  3  (author_and_software_defined_assembly)    
Structural data PDB
Oligomeric count 1
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others J (18IStructure of 18I18I )
Each chain information
Chain C heme  
auth_asym_id C
Residue indices (Uniprot) 29-478 (32-481)
Mutations (UniProt numbering)
Uniprot ID Q385E8 →UniprotKB
label_asym_ids of heme I
Available structure PDB
Assembly ID:  4  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 1
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others L (18IStructure of 18I18I )
Each chain information
Chain D heme  
auth_asym_id D
Residue indices (Uniprot) 29-478 (32-481)
Mutations (UniProt numbering)
Missing residues 251ALA-256SER
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 0.17 Å