3OA8
Diheme SoxAX
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016669 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor |
| A | 0019417 | biological_process | sulfur oxidation |
| A | 0020037 | molecular_function | heme binding |
| A | 0070069 | cellular_component | cytochrome complex |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0020037 | molecular_function | heme binding |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0016669 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor |
| C | 0019417 | biological_process | sulfur oxidation |
| C | 0020037 | molecular_function | heme binding |
| C | 0070069 | cellular_component | cytochrome complex |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0020037 | molecular_function | heme binding |
| E | 0009055 | molecular_function | electron transfer activity |
| E | 0016669 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor |
| E | 0019417 | biological_process | sulfur oxidation |
| E | 0020037 | molecular_function | heme binding |
| E | 0070069 | cellular_component | cytochrome complex |
| F | 0009055 | molecular_function | electron transfer activity |
| F | 0020037 | molecular_function | heme binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEC A 401 |
| Chain | Residue |
| A | PHE181 |
| A | THR212 |
| A | TRP216 |
| A | MET233 |
| A | CSS236 |
| A | TYR237 |
| A | GLN239 |
| A | MET240 |
| A | LYS274 |
| A | HOH536 |
| A | HOH826 |
| A | SER182 |
| A | CYS183 |
| A | CYS186 |
| A | HIS187 |
| A | ILE194 |
| A | GLN197 |
| A | ALA198 |
| A | LEU199 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEC B 401 |
| Chain | Residue |
| A | PHE181 |
| B | CYS125 |
| B | CYS128 |
| B | HIS129 |
| B | LEU141 |
| B | PRO143 |
| B | LEU145 |
| B | TYR148 |
| B | LYS165 |
| B | VAL166 |
| B | SER176 |
| B | MET178 |
| B | PRO179 |
| B | VAL195 |
| B | HOH222 |
| B | HOH372 |
| F | GLU74 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 209 |
| Chain | Residue |
| B | ASN70 |
| B | PRO71 |
| D | ASN70 |
| D | PRO71 |
| F | ASN70 |
| F | PRO71 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEC C 401 |
| Chain | Residue |
| C | SER182 |
| C | CYS183 |
| C | CYS186 |
| C | HIS187 |
| C | ILE194 |
| C | GLN197 |
| C | LEU199 |
| C | THR212 |
| C | TRP216 |
| C | ARG232 |
| C | MET233 |
| C | CSS236 |
| C | TYR237 |
| C | GLN239 |
| C | MET240 |
| C | LYS274 |
| C | HOH835 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEC D 401 |
| Chain | Residue |
| B | GLU74 |
| C | PHE181 |
| D | GLY123 |
| D | ASN124 |
| D | CYS125 |
| D | CYS128 |
| D | HIS129 |
| D | LEU141 |
| D | PRO143 |
| D | LEU145 |
| D | TYR148 |
| D | ARG152 |
| D | LYS165 |
| D | VAL166 |
| D | SER176 |
| D | MET178 |
| D | HOH227 |
| D | HOH576 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEC E 401 |
| Chain | Residue |
| E | SER182 |
| E | CYS183 |
| E | CYS186 |
| E | HIS187 |
| E | ILE194 |
| E | GLN197 |
| E | THR212 |
| E | MET213 |
| E | TRP216 |
| E | ARG232 |
| E | MET233 |
| E | CSS236 |
| E | TYR237 |
| E | MET240 |
| E | LYS274 |
| E | HOH346 |
| E | HOH452 |
| site_id | AC7 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC F 401 |
| Chain | Residue |
| F | LEU141 |
| F | PRO143 |
| F | LEU145 |
| F | TYR148 |
| F | ARG152 |
| F | LYS165 |
| F | VAL166 |
| F | LEU173 |
| F | SER176 |
| F | SER177 |
| F | MET178 |
| F | PRO179 |
| F | PHE181 |
| F | HOH241 |
| F | HOH529 |
| F | HOH592 |
| D | GLU74 |
| E | PHE181 |
| F | CYS125 |
| F | CYS128 |
| F | HIS129 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Cysteine persulfide intermediate","evidences":[{"source":"PubMed","id":"21592966","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21592966","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21592966","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q939U1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






