2OZ1
The SoxAX Complex of Rhodovulum Sulfidophilum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004792 | molecular_function | thiosulfate-cyanide sulfurtransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016669 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016783 | molecular_function | sulfurtransferase activity |
| A | 0019417 | biological_process | sulfur oxidation |
| A | 0019418 | biological_process | sulfide oxidation |
| A | 0020037 | molecular_function | heme binding |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046982 | molecular_function | protein heterodimerization activity |
| A | 0070069 | cellular_component | cytochrome complex |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0020037 | molecular_function | heme binding |
| C | 0004792 | molecular_function | thiosulfate-cyanide sulfurtransferase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016669 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016783 | molecular_function | sulfurtransferase activity |
| C | 0019417 | biological_process | sulfur oxidation |
| C | 0019418 | biological_process | sulfide oxidation |
| C | 0020037 | molecular_function | heme binding |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0046982 | molecular_function | protein heterodimerization activity |
| C | 0070069 | cellular_component | cytochrome complex |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0020037 | molecular_function | heme binding |
| E | 0004792 | molecular_function | thiosulfate-cyanide sulfurtransferase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0009055 | molecular_function | electron transfer activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016669 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor |
| E | 0016740 | molecular_function | transferase activity |
| E | 0016783 | molecular_function | sulfurtransferase activity |
| E | 0019417 | biological_process | sulfur oxidation |
| E | 0019418 | biological_process | sulfide oxidation |
| E | 0020037 | molecular_function | heme binding |
| E | 0042597 | cellular_component | periplasmic space |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0046982 | molecular_function | protein heterodimerization activity |
| E | 0070069 | cellular_component | cytochrome complex |
| F | 0009055 | molecular_function | electron transfer activity |
| F | 0020037 | molecular_function | heme binding |
| G | 0004792 | molecular_function | thiosulfate-cyanide sulfurtransferase activity |
| G | 0005515 | molecular_function | protein binding |
| G | 0009055 | molecular_function | electron transfer activity |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016669 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor |
| G | 0016740 | molecular_function | transferase activity |
| G | 0016783 | molecular_function | sulfurtransferase activity |
| G | 0019417 | biological_process | sulfur oxidation |
| G | 0019418 | biological_process | sulfide oxidation |
| G | 0020037 | molecular_function | heme binding |
| G | 0042597 | cellular_component | periplasmic space |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0046982 | molecular_function | protein heterodimerization activity |
| G | 0070069 | cellular_component | cytochrome complex |
| H | 0009055 | molecular_function | electron transfer activity |
| H | 0020037 | molecular_function | heme binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEC A 952 |
| Chain | Residue |
| A | ALA75 |
| A | CYS114 |
| A | ARG118 |
| A | MET119 |
| A | HOH982 |
| A | CYS76 |
| A | CYS79 |
| A | HIS80 |
| A | MET87 |
| A | LEU90 |
| A | TYR94 |
| A | SER100 |
| A | ILE111 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEC A 953 |
| Chain | Residue |
| A | GLY34 |
| A | ARG38 |
| A | LEU175 |
| A | SER176 |
| A | CYS177 |
| A | CYS180 |
| A | HIS181 |
| A | ILE189 |
| A | ASP192 |
| A | HIS193 |
| A | SER195 |
| A | GLN198 |
| A | ILE199 |
| A | PHE202 |
| A | ARG218 |
| A | PHE219 |
| A | CSS222 |
| A | ILE223 |
| A | ARG260 |
| A | ASN261 |
| A | HOH958 |
| A | HOH975 |
| A | HOH1010 |
| A | HOH1020 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEC B 951 |
| Chain | Residue |
| A | TYR184 |
| A | HOH970 |
| B | GLY40 |
| B | ASN41 |
| B | CYS42 |
| B | CYS45 |
| B | HIS46 |
| B | PRO62 |
| B | LEU64 |
| B | VAL67 |
| B | ARG70 |
| B | TYR71 |
| B | ILE79 |
| B | LEU80 |
| B | PHE87 |
| B | THR90 |
| B | VAL91 |
| B | MET92 |
| B | PRO93 |
| B | TYR95 |
| B | VAL129 |
| B | HOH1004 |
| B | HOH1019 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEC C 952 |
| Chain | Residue |
| C | LYS74 |
| C | ALA75 |
| C | CYS76 |
| C | CYS79 |
| C | HIS80 |
| C | MET87 |
| C | LEU90 |
| C | TYR94 |
| C | SER100 |
| C | MET110 |
| C | ILE111 |
| C | CYS114 |
| C | ARG115 |
| C | ARG118 |
| C | MET119 |
| C | HOH968 |
| C | HOH1026 |
| C | HOH1080 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEC C 953 |
| Chain | Residue |
| C | ASN261 |
| C | HOH975 |
| C | HOH1038 |
| C | HOH1086 |
| C | HOH1094 |
| C | GLY34 |
| C | ARG38 |
| C | LEU175 |
| C | SER176 |
| C | CYS177 |
| C | CYS180 |
| C | HIS181 |
| C | ILE189 |
| C | ASP192 |
| C | HIS193 |
| C | LEU194 |
| C | SER195 |
| C | GLY197 |
| C | GLN198 |
| C | ILE199 |
| C | PHE202 |
| C | ARG218 |
| C | PHE219 |
| C | CSS222 |
| C | ILE223 |
| C | ARG260 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC D 951 |
| Chain | Residue |
| C | TYR184 |
| C | HOH1104 |
| D | CYS42 |
| D | CYS45 |
| D | HIS46 |
| D | VAL60 |
| D | GLY61 |
| D | PRO62 |
| D | LEU64 |
| D | ARG70 |
| D | TYR71 |
| D | LEU80 |
| D | PHE87 |
| D | THR90 |
| D | VAL91 |
| D | MET92 |
| D | PRO93 |
| D | TYR95 |
| D | MET121 |
| D | VAL129 |
| D | LEU133 |
| D | HOH966 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEC E 952 |
| Chain | Residue |
| E | CYS76 |
| E | CYS79 |
| E | HIS80 |
| E | LEU90 |
| E | TYR94 |
| E | SER100 |
| E | MET110 |
| E | ILE111 |
| E | CYS114 |
| E | ARG115 |
| E | ARG118 |
| E | MET119 |
| E | HOH954 |
| E | HOH1014 |
| H | GLU114 |
| site_id | AC8 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE HEC E 953 |
| Chain | Residue |
| E | GLY34 |
| E | ARG38 |
| E | LEU175 |
| E | SER176 |
| E | CYS177 |
| E | CYS180 |
| E | HIS181 |
| E | ASP192 |
| E | HIS193 |
| E | LEU194 |
| E | SER195 |
| E | GLY197 |
| E | GLN198 |
| E | ILE199 |
| E | PHE202 |
| E | ARG218 |
| E | PHE219 |
| E | CSS222 |
| E | ILE223 |
| E | ARG260 |
| E | ASN261 |
| E | HOH977 |
| E | HOH986 |
| E | HOH994 |
| E | HOH1067 |
| E | HOH1136 |
| E | HOH1143 |
| site_id | AC9 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEC F 951 |
| Chain | Residue |
| E | TYR184 |
| E | HOH1006 |
| F | GLY40 |
| F | CYS42 |
| F | CYS45 |
| F | HIS46 |
| F | VAL60 |
| F | GLY61 |
| F | PRO62 |
| F | LEU64 |
| F | ARG70 |
| F | TYR71 |
| F | ILE79 |
| F | LEU80 |
| F | PHE87 |
| F | THR90 |
| F | VAL91 |
| F | MET92 |
| F | PRO93 |
| F | TYR95 |
| F | VAL129 |
| F | HOH973 |
| F | HOH1013 |
| site_id | BC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEC G 952 |
| Chain | Residue |
| G | ALA75 |
| G | CYS76 |
| G | CYS79 |
| G | HIS80 |
| G | MET87 |
| G | LEU90 |
| G | TYR94 |
| G | SER100 |
| G | ILE111 |
| G | CYS114 |
| G | ARG118 |
| G | MET119 |
| G | HOH975 |
| G | HOH1055 |
| site_id | BC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC G 953 |
| Chain | Residue |
| G | GLY34 |
| G | ARG38 |
| G | SER176 |
| G | CYS177 |
| G | CYS180 |
| G | HIS181 |
| G | ILE189 |
| G | ASP192 |
| G | HIS193 |
| G | SER195 |
| G | GLN198 |
| G | ILE199 |
| G | PHE202 |
| G | ARG218 |
| G | PHE219 |
| G | CSS222 |
| G | ILE223 |
| G | ARG260 |
| G | HOH956 |
| G | HOH960 |
| G | HOH965 |
| G | HOH1071 |
| site_id | BC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC H 951 |
| Chain | Residue |
| G | TYR184 |
| G | HOH1021 |
| H | ASN41 |
| H | CYS42 |
| H | CYS45 |
| H | HIS46 |
| H | PRO62 |
| H | LEU64 |
| H | ARG70 |
| H | TYR71 |
| H | LEU80 |
| H | PHE87 |
| H | THR90 |
| H | VAL91 |
| H | MET92 |
| H | PRO93 |
| H | TYR95 |
| H | MET121 |
| H | VAL129 |
| H | HOH990 |
| H | HOH1012 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 376 |
| Details | Domain: {"description":"Cytochrome c","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Cysteine persulfide intermediate","evidences":[{"source":"PubMed","id":"12411478","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23060437","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12411478","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23060437","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12411478","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23060437","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12411478","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
