Danish
Uniprot ID:  P26287
  • Protein: Cytochrome f
  • Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
  • Length: 328
  • Sequence:
    • MRNPDTLGLWTKTMVALRRFTVLAIATVSVFLITDLGLPQAASAYPFWAQETAPLTPREATGRIVCANCHLAQKAAEVEIPQAVLPDTVFEAVVKIPYDLDSQQVLGDGSKGGLNVGAVLMLPEGFKIAPPDRLSEGLKEKVGGTYFQPYREDMENVVIVGPLPGEQYQEIVFPVLSPDPAKDKSINYGKFAVHLGANRGRGQIYPTGLLSNNNAFKAPNAGTISEVNALEAGGYQLILTTADGTETVDIPAGPELIVSAGQTVEAGEFLTNNPNVGGFGQKDTEVVLQNPTRIKFLVLFLAGIMLSQILLVLKKKQIEKVQAAELNF
Exclude chains with
Mutations (vs. UniProt)
Clear
Number of chains:  4
PDB ID:  pdb_00007r0w , Chain D 
Residue indices (Uniprot), coverage 1-285 (1-328), 1.00
Mutations (UniProt numbering) None
Insertions None
Deletions None
Sequence identity to UniProt 1.0000
auth_asym_id K
Missing residues 195LEU-199ASP
Structural gaps Exists
label_asym_ids of heme AA
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.16 Å
PDB ID:  pdb_00007r0w , Chain K 
Residue indices (Uniprot), coverage 1-285 (1-328), 1.00
Mutations (UniProt numbering) None
Insertions None
Deletions None
Sequence identity to UniProt 1.0000
auth_asym_id C
Missing residues 195LEU-199ASP
Structural gaps Exists
label_asym_ids of heme MA
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.17 Å
PDB ID:  pdb_00007zxy , Chain C 
Residue indices (Uniprot), coverage 1-285 (45-328), 0.87
Mutations (UniProt numbering) None
Insertions None
Deletions M1-A44
Sequence identity to UniProt 1.0000
auth_asym_id C
Missing residues 195LEU-199ASP
Structural gaps Exists
label_asym_ids of heme X
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å
PDB ID:  pdb_00007zxy , Chain K 
Residue indices (Uniprot), coverage 1-285 (45-328), 0.87
Mutations (UniProt numbering) None
Insertions None
Deletions M1-A44
Sequence identity to UniProt 1.0000
auth_asym_id K
Missing residues 195LEU-199ASP
Structural gaps Exists
label_asym_ids of heme LA
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å