2BQ4
Crystal structure of type I cytochrome c3 from Desulfovibrio africanus
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 |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0009061 | biological_process | anaerobic respiration |
| B | 0020037 | molecular_function | heme binding |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A1119 |
| Chain | Residue |
| A | ASP10 |
| A | LEU12 |
| A | GLU20 |
| A | TYR21 |
| A | HEC1118 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B1120 |
| Chain | Residue |
| B | HEC1119 |
| B | ASP10 |
| B | LEU12 |
| B | GLU20 |
| B | TYR21 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEC A1115 |
| Chain | Residue |
| A | PRO1 |
| A | GLN2 |
| A | VAL3 |
| A | PRO4 |
| A | HIS11 |
| A | PHE25 |
| A | HIS27 |
| A | HIS30 |
| A | ALA39 |
| A | CYS40 |
| A | CYS43 |
| A | HIS44 |
| A | GLY54 |
| A | HEC1117 |
| A | HOH2130 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEC A1116 |
| Chain | Residue |
| A | CYS43 |
| A | HIS44 |
| A | HIS45 |
| A | LYS46 |
| A | CYS56 |
| A | GLU59 |
| A | GLY60 |
| A | CYS61 |
| A | HIS62 |
| A | ALA81 |
| A | SER84 |
| A | SER86 |
| A | MET88 |
| A | SER89 |
| A | HOH2131 |
| A | HOH2132 |
| A | HOH2133 |
| B | LYS28 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEC A1117 |
| Chain | Residue |
| A | PHE25 |
| A | ALA29 |
| A | HIS30 |
| A | SER32 |
| A | LEU33 |
| A | THR35 |
| A | CYS43 |
| A | PRO87 |
| A | MET88 |
| A | SER89 |
| A | CYS90 |
| A | CYS93 |
| A | HIS94 |
| A | MET97 |
| A | THR103 |
| A | THR104 |
| A | GLY105 |
| A | PRO106 |
| A | HEC1115 |
| A | HOH2134 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEC A1118 |
| Chain | Residue |
| A | ILE9 |
| A | ASP10 |
| A | HIS11 |
| A | LEU12 |
| A | SER13 |
| A | ASN14 |
| A | LEU19 |
| A | GLU20 |
| A | TYR21 |
| A | VAL23 |
| A | PHE68 |
| A | ALA70 |
| A | MET79 |
| A | PHE82 |
| A | HIS83 |
| A | CYS90 |
| A | GLN91 |
| A | HIS94 |
| A | PRO106 |
| A | THR107 |
| A | CYS109 |
| A | CYS112 |
| A | HIS113 |
| A | CA1119 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEC B1116 |
| Chain | Residue |
| B | HEC1118 |
| B | HOH2010 |
| B | HOH2081 |
| B | HOH2141 |
| B | HOH2142 |
| B | HOH2143 |
| B | HOH2144 |
| B | HOH2145 |
| B | GLN2 |
| B | HIS11 |
| B | PHE25 |
| B | HIS27 |
| B | HIS30 |
| B | ALA39 |
| B | CYS40 |
| B | CYS43 |
| B | HIS44 |
| B | ILE53 |
| B | GLY54 |
| B | GLY55 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEC B1117 |
| Chain | Residue |
| A | LYS28 |
| B | CYS43 |
| B | HIS45 |
| B | LYS46 |
| B | GLY55 |
| B | CYS56 |
| B | GLU59 |
| B | GLY60 |
| B | CYS61 |
| B | HIS62 |
| B | PRO75 |
| B | ALA81 |
| B | SER84 |
| B | SER86 |
| B | MET88 |
| B | SER89 |
| B | HOH2146 |
| B | HOH2147 |
| site_id | AC9 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC B1118 |
| Chain | Residue |
| B | PHE25 |
| B | ALA29 |
| B | HIS30 |
| B | SER32 |
| B | LEU33 |
| B | THR35 |
| B | CYS43 |
| B | PRO87 |
| B | SER89 |
| B | CYS90 |
| B | CYS93 |
| B | HIS94 |
| B | MET97 |
| B | THR103 |
| B | THR104 |
| B | GLY105 |
| B | PRO106 |
| B | GLN115 |
| B | HEC1116 |
| B | HOH2148 |
| B | HOH2149 |
| site_id | BC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEC B1119 |
| Chain | Residue |
| B | ILE9 |
| B | ASP10 |
| B | HIS11 |
| B | LEU12 |
| B | SER13 |
| B | ASN14 |
| B | LEU19 |
| B | GLU20 |
| B | TYR21 |
| B | VAL23 |
| B | PHE68 |
| B | ALA70 |
| B | MET79 |
| B | PHE82 |
| B | HIS83 |
| B | CYS90 |
| B | GLN91 |
| B | HIS94 |
| B | PRO106 |
| B | THR107 |
| B | CYS109 |
| B | CYS112 |
| B | HIS113 |
| B | CA1120 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16226767","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BQ4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"16226767","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BQ4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"16226767","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BQ4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
