PDB ID:  pdb_00006h08
  • The crystal structure of engineered cytochrome c peroxidase from Saccharomyces cerevisiae with a His175Me-His proximal ligand substitution
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 1.9 Å
  • Deposition date: 2018-07-06
Number of assemblies:  3
Assembly ID:  1  (author_defined_assembly)    
Structural data modeled
Oligomeric count 1
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others E (COStructure of COCO ), F (MNStructure of MNMN ), G (NAStructure of NANA )
Each chain information
Chain A heme  
auth_asym_id A
Residue indices (Uniprot) 0-294 (71-361)
Mutations (UniProt numbering)
Missing residues 175HIS-175HIS
Nonstandard amino acids Structure of MHSMHS
Uniprot ID P00431 →UniprotKB
label_asym_ids of heme D
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.10 Å
Assembly ID:  2  (author_defined_assembly)    
Structural data modeled
Oligomeric count 1
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others H (NAStructure of NANA ), J (COStructure of COCO ), K (COStructure of COCO )
Each chain information
Chain B heme  
auth_asym_id B
Residue indices (Uniprot) -2-294 (71-361)
Mutations (UniProt numbering)
Missing residues 175HIS-175HIS
Nonstandard amino acids Structure of MHSMHS
Uniprot ID P00431 →UniprotKB
label_asym_ids of heme I
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.10 Å
Assembly ID:  3  (author_defined_assembly)    
Structural data modeled
Oligomeric count 1
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others M (COStructure of COCO ), N (COStructure of COCO ), O (COStructure of COCO )
Each chain information
Chain C heme  
auth_asym_id C
Residue indices (Uniprot) -2-294 (71-361)
Mutations (UniProt numbering)
Missing residues 175HIS-175HIS
Nonstandard amino acids Structure of MHSMHS
Uniprot ID P00431 →UniprotKB
label_asym_ids of heme L
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.10 Å