PDB ID:  pdb_00001zzh
  • Structure of the fully oxidized di-heme cytochrome c peroxidase from R. capsulatus
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 2.7 Å
  • Deposition date: 2005-06-14
Number of assemblies:  2
Assembly ID:  1  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 2
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others E (CAStructure of CACA ), F (ZNStructure of ZNZN ), G (ZNStructure of ZNZN ), U (CAStructure of CACA ), V (ZNStructure of ZNZN )
Each chain information
Chain A heme  
auth_asym_id A
Residue indices (Uniprot) 4-326 (-)
Missing residues 22GLN-28THR:109LYS-117GLU:224GLY-233LYS
Structural gaps Exists
Uniprot ID Unavailable
label_asym_ids of heme I ,  H
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.18 Å
Chain D heme  
auth_asym_id D
Residue indices (Uniprot) 4-326 (-)
Missing residues 23LEU-28THR:109LYS-117GLU:224GLY-233LYS
Structural gaps Exists
Uniprot ID Unavailable
label_asym_ids of heme X ,  W
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.18 Å
Assembly ID:  2  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 2
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others J (CAStructure of CACA ), K (ZNStructure of ZNZN ), L (ZNStructure of ZNZN ), M (ZNStructure of ZNZN ), N (ZNStructure of ZNZN ), Q (CAStructure of CACA ), R (ZNStructure of ZNZN )
Each chain information
Chain B heme  
auth_asym_id B
Residue indices (Uniprot) 4-326 (-)
Missing residues 23LEU-26ASN:109LYS-117GLU:230ALA-231GLY
Structural gaps Exists
Uniprot ID Unavailable
label_asym_ids of heme P ,  O
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.15 Å
Chain C heme  
auth_asym_id C
Residue indices (Uniprot) 4-326 (-)
Missing residues 23LEU-26ASN:109LYS-117GLU:231GLY-233LYS
Structural gaps Exists
Uniprot ID Unavailable
label_asym_ids of heme T ,  S
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.18 Å