Danish
Uniprot ID:  Q749D0
  • Protein: Cytochrome c peroxidase
  • Organism: Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
  • Length: 345
  • Sequence:
    • MKQLSVSLAILCAVATSEAFAADELQQRAQGLFKPVPAKAPTLKGNPASPVKVELGKMLYFDPRLSASHLISCNTCHNVGLGGGDLQATSTGHGWQKGPRNAPTVLNSVFNTAQFWDGRAKDLAEQAKGPVQASVEMNNTPDQVVKTLNSIPDYVALFKKAFPGEKDPVTFDNMAKAIEVFEATLITPDSPFDQYLKGKKKALDGKQTAGLKLFLDKGCVACHGGLNLGGTGYFPFGVVEKPAENILPLGDKGRFAVTNTAKDEYVFRAPSLRNVAITYPYFHSGVVWSLKEAVAVMGSAQFGIKLSDDESEAIAAFLGSLTGKQPKVVYPIMPASTDATPRPRL
Exclude chains with
Mutations (vs. UniProt)
Clear
Number of chains:  8
PDB ID:  pdb_00003hq9 , Chain A 
Resolution 1.52 Å
Residue indices (Uniprot), coverage 22-345 (1-345), 1.00
Difference from Uniprot sequence engineered mutation
Mutations (UniProt numbering) S134P
Insertions None
Deletions None
Sequence identity to UniProt 0.9971
auth_asym_id A
Missing residues 241LYS-252LYS
Structural gaps Exists
label_asym_ids of heme D ,  C
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.07 Å
PDB ID:  pdb_00003hq9 , Chain B 
Resolution 1.52 Å
Residue indices (Uniprot), coverage 21-345 (1-345), 1.00
Difference from Uniprot sequence engineered mutation
Mutations (UniProt numbering) S134P
Insertions None
Deletions None
Sequence identity to UniProt 0.9971
auth_asym_id B
Missing residues 124ALA-131VAL:242PRO-252LYS
Structural gaps Exists
label_asym_ids of heme L ,  K
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.11 Å
PDB ID:  pdb_00003hq6 , Chain A 
Resolution 2.00 Å
Residue indices (Uniprot), coverage 22-345 (1-345), 1.00
Mutations (UniProt numbering) None
Insertions None
Deletions None
Sequence identity to UniProt 1.0000
auth_asym_id A
label_asym_ids of heme D ,  C
Available structure PDB
PDB ID:  pdb_00003hq6 , Chain B 
Resolution 2.00 Å
Residue indices (Uniprot), coverage 22-345 (1-345), 1.00
Mutations (UniProt numbering) None
Insertions None
Deletions None
Sequence identity to UniProt 1.0000
auth_asym_id B
Missing residues 242PRO-252LYS
Structural gaps Exists
label_asym_ids of heme G ,  F
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å
PDB ID:  pdb_00003hq7 , Chain A 
Resolution 2.31 Å
Residue indices (Uniprot), coverage 20-345 (1-345), 1.00
Difference from Uniprot sequence engineered mutation
Mutations (UniProt numbering) G94K, K97Q, R100I
Insertions None
Deletions None
Sequence identity to UniProt 0.9913
auth_asym_id A
Missing residues 114GLN-126GLN:243ALA-251ASP
Structural gaps Exists
label_asym_ids of heme C ,  B
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.29 Å
PDB ID:  pdb_00003hq7 , Chain A-1 
Resolution 2.31 Å
Residue indices (Uniprot), coverage 20-345 (1-345), 1.00
Difference from Uniprot sequence engineered mutation
Mutations (UniProt numbering) G94K, K97Q, R100I
Insertions None
Deletions None
Sequence identity to UniProt 0.9913
auth_asym_id A
Missing residues 114GLN-126GLN:243ALA-251ASP
Structural gaps Exists
label_asym_ids of heme C-1 ,  B-1
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.31 Å
PDB ID:  pdb_00003hq8 , Chain A 
Resolution 2.40 Å
Residue indices (Uniprot), coverage 22-345 (1-345), 1.00
Difference from Uniprot sequence engineered mutation
Mutations (UniProt numbering) S134P, V135K
Insertions None
Deletions None
Sequence identity to UniProt 0.9942
auth_asym_id A
Missing residues 244GLU-252LYS
Structural gaps Exists
label_asym_ids of heme D ,  C
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
PDB ID:  pdb_00003hq8 , Chain B 
Resolution 2.40 Å
Residue indices (Uniprot), coverage 22-345 (1-345), 1.00
Difference from Uniprot sequence engineered mutation
Mutations (UniProt numbering) S134P, V135K
Insertions None
Deletions None
Sequence identity to UniProt 0.9942
auth_asym_id B
Missing residues 242PRO-252LYS
Structural gaps Exists
label_asym_ids of heme H ,  G
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 1.19 Å