Uniprot ID:  D5ARP7
  • Protein: Cbb3-type cytochrome c oxidase subunit CcoP
  • Organism: Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
  • Length: 297
  • Sequence:
  • MSKKPTTKKEVQTTGHSWDGIEELNTPLPRWWLWTFYATIVWGVAYSIAMPAWPIFASGATPGILGSSTRADVEKDIAKFAEMNKAVEDKLVATDLTAIAADPELVTYTRNAGAAVFRTWCAQCHGAGAGGNTGFPSLLDGDWLHGGSIETIYTNIKHGIRDPLDPDTLPVANMPAHLTDELLEPAQIDDVVQYVLKISGQPADEARATAGQQVFADNCVSCHGEDAKGMVEMGAPNLTDGIWLYGGDANTITTTIQLGRGGVMPSWSWAADGAKPRLSEAQIRAVASYVHSLGGGQ
Exclude chains with
Mutations (vs. UniProt)
Number of chains:  3
PDB ID:  pdb_00006xkw , Chain C 
Residue indices (Uniprot), coverage 13-295 (1-297), 1.00
Mutations (UniProt numbering) None
Insertions None
Deletions None
Sequence identity to UniProt 1.0000
auth_asym_id p
Missing residues 53TRP-59GLY:161ARG-173ASN:272ASP-280GLU
Structural gaps Exists
label_asym_ids of heme Q ,  P
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.26 Å
PDB ID:  pdb_00006xkx , Chain I 
Residue indices (Uniprot), coverage 13-295 (1-297), 1.00
Mutations (UniProt numbering) None
Insertions 297insLFATRPATAVAVGADGKALLPSVDEAAMPAKAPAAAAPAAETAEAAAPAEPAAPPPPAYVEVDPATITGDAKAGEEKFNKTCKACHKIDGKNAVGPHLNGVIGRATATVEGFKYSTAMKNHVGNWTPERLDIYLVSPKAEVPGTKMSFVGLPEAADRANVIAYLNTLPRDYKDDDDK
Deletions None
Sequence identity to UniProt 1.0000
auth_asym_id p
Missing residues 53TRP-59GLY:161ARG-173ASN:272ASP-280GLU
Structural gaps Exists
label_asym_ids of heme W ,  V
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.24 Å
PDB ID:  pdb_00006xkz , Chain I 
Residue indices (Uniprot), coverage 13-295 (1-297), 1.00
Mutations (UniProt numbering) None
Insertions 297insLFATRPATAVAVGADGKALLPSVDEAAMPAKAPAAAAPAAETAEAAAPAEPAAPPPPAYVEVDPATITGDAKAGEEKFNKTCKACHKIDGKNAVGPHLNGVIGRATATVEGFKYSTAMKNHVGNWTPERLDIYLVSPKAEVPGTKMSFVGLPEAADRANVIAYLNTLPRDYKDDDDK
Deletions None
Sequence identity to UniProt 1.0000
auth_asym_id p
Missing residues 53TRP-59GLY:161ARG-173ASN:272ASP-280GLU
Structural gaps Exists
label_asym_ids of heme W ,  V
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.25 Å