Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0009055 | molecular_function | electron transfer activity |
A | 0009061 | biological_process | anaerobic respiration |
A | 0020037 | molecular_function | heme binding |
A | 0042597 | cellular_component | periplasmic space |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM A 108 |
Chain | Residue |
A | MET11 |
A | CYS79 |
A | HIS83 |
A | LEU97 |
A | GLY99 |
A | CYS100 |
A | CYS105 |
A | HIS106 |
A | HOH120 |
A | HOH148 |
A | HOH149 |
A | GLU12 |
A | ALA13 |
A | THR14 |
A | GLN16 |
A | LYS29 |
A | TYR65 |
A | TYR66 |
A | HIS70 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE HEM A 109 |
Chain | Residue |
A | CYS33 |
A | HIS35 |
A | ASP42 |
A | ARG44 |
A | LYS45 |
A | CYS46 |
A | CYS51 |
A | HIS52 |
A | HIS67 |
A | THR74 |
A | LYS75 |
A | PHE76 |
A | HOH115 |
A | HOH126 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HEM A 110 |
Chain | Residue |
A | LYS3 |
A | PRO5 |
A | PHE20 |
A | HIS22 |
A | HIS25 |
A | VAL28 |
A | LYS29 |
A | CYS30 |
A | CYS33 |
A | HIS34 |
A | TYR43 |
A | LYS45 |
A | CYS46 |
A | HEM111 |
A | HOH125 |
A | HOH145 |
A | HOH147 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HEM A 111 |
Chain | Residue |
A | ASN21 |
A | THR24 |
A | HIS25 |
A | VAL28 |
A | SER78 |
A | CYS79 |
A | CYS82 |
A | HIS83 |
A | LYS93 |
A | LEU97 |
A | LYS104 |
A | HEM110 |
A | HOH117 |
A | HOH143 |
A | HOH144 |
A | HOH148 |
A | HOH150 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | Binding site: {"description":"axial binding residue"} |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | Binding site: {"description":"covalent"} |