3MMA
Dissimilatory sulfite reductase phosphate complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0018551 | molecular_function | dissimilatory sulfite reductase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0006790 | biological_process | sulfur compound metabolic process |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0018551 | molecular_function | dissimilatory sulfite reductase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0018551 | molecular_function | dissimilatory sulfite reductase activity |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| E | 0006790 | biological_process | sulfur compound metabolic process |
| E | 0009055 | molecular_function | electron transfer activity |
| E | 0016020 | cellular_component | membrane |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0018551 | molecular_function | dissimilatory sulfite reductase activity |
| E | 0020037 | molecular_function | heme binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051536 | molecular_function | iron-sulfur cluster binding |
| E | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE SRM A 580 |
| Chain | Residue |
| A | ARG80 |
| A | LYS211 |
| A | LYS213 |
| A | LYS215 |
| A | ARG229 |
| A | LYS314 |
| A | ALA315 |
| A | PHE317 |
| A | ARG358 |
| A | ARG360 |
| A | HOH454 |
| A | ARG98 |
| A | PO4590 |
| B | ARG60 |
| B | THR134 |
| B | GLN135 |
| B | HIS139 |
| B | HIS141 |
| B | THR142 |
| B | ASN180 |
| B | CYS182 |
| B | GLY183 |
| A | GLY131 |
| B | THR249 |
| B | SF4585 |
| A | SER132 |
| A | THR133 |
| A | GLY134 |
| A | ASP135 |
| A | ILE137 |
| A | TYR210 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 A 575 |
| Chain | Residue |
| A | CYS175 |
| A | CYS181 |
| A | PHE183 |
| A | ALA184 |
| A | GLY218 |
| A | CYS219 |
| A | ASN221 |
| A | CYS223 |
| B | SRM570 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 A 576 |
| Chain | Residue |
| A | CYS266 |
| A | PRO267 |
| A | THR268 |
| A | CYS285 |
| A | VAL286 |
| A | CYS288 |
| A | MET289 |
| A | CYS291 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 590 |
| Chain | Residue |
| A | ARG98 |
| A | ARG170 |
| A | LYS211 |
| A | LYS213 |
| A | HOH489 |
| A | SRM580 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 B 585 |
| Chain | Residue |
| A | SRM580 |
| B | THR134 |
| B | CYS140 |
| B | THR142 |
| B | PRO143 |
| B | CYS177 |
| B | CYS178 |
| B | ASN180 |
| B | CYS182 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 B 586 |
| Chain | Residue |
| B | CYS220 |
| B | THR222 |
| B | LEU225 |
| B | CYS241 |
| B | MET242 |
| B | CYS244 |
| B | GLY245 |
| B | CYS247 |
| B | LEU256 |
| site_id | AC7 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE SRM B 570 |
| Chain | Residue |
| B | ARG276 |
| B | ARG319 |
| B | HOH368 |
| B | HOH382 |
| B | HOH385 |
| B | HOH388 |
| B | HOH396 |
| A | CYS175 |
| A | MET176 |
| A | CYS181 |
| A | GLU182 |
| A | PHE183 |
| A | ASN221 |
| A | CYS223 |
| A | ASN293 |
| A | SF4575 |
| B | HIS33 |
| B | ILE41 |
| B | ARG43 |
| B | ARG55 |
| B | ARG83 |
| B | THR85 |
| B | SER86 |
| B | ARG87 |
| B | ASN89 |
| B | GLY117 |
| B | THR118 |
| B | TRP119 |
| B | ALA121 |
| B | SER129 |
| B | MET170 |
| B | ARG172 |
| B | LEU272 |
| B | SER273 |
| site_id | AC8 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE SRM D 580 |
| Chain | Residue |
| D | ILE78 |
| D | ARG80 |
| D | THR96 |
| D | ARG98 |
| D | GLY131 |
| D | SER132 |
| D | THR133 |
| D | GLY134 |
| D | ASP135 |
| D | TYR210 |
| D | LYS211 |
| D | LYS213 |
| D | LYS215 |
| D | ARG229 |
| D | LYS314 |
| D | ALA315 |
| D | PHE317 |
| D | ARG358 |
| D | ARG360 |
| E | ARG60 |
| E | THR134 |
| E | GLN135 |
| E | HIS139 |
| E | HIS141 |
| E | ASN180 |
| E | CYS182 |
| E | GLY183 |
| E | THR249 |
| E | SF4585 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 D 575 |
| Chain | Residue |
| D | CYS175 |
| D | MET176 |
| D | CYS181 |
| D | PHE183 |
| D | ALA184 |
| D | GLY218 |
| D | CYS219 |
| D | ASN221 |
| D | ASP222 |
| D | CYS223 |
| E | SRM570 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SF4 D 576 |
| Chain | Residue |
| D | CYS266 |
| D | CYS285 |
| D | VAL286 |
| D | CYS288 |
| D | MET289 |
| D | CYS291 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 E 585 |
| Chain | Residue |
| D | SRM580 |
| E | THR134 |
| E | GLN135 |
| E | CYS140 |
| E | PRO143 |
| E | CYS177 |
| E | CYS178 |
| E | ASN180 |
| E | CYS182 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 E 586 |
| Chain | Residue |
| E | CYS220 |
| E | THR222 |
| E | LEU225 |
| E | CYS241 |
| E | MET242 |
| E | CYS244 |
| E | GLY245 |
| E | CYS247 |
| site_id | BC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE SRM E 570 |
| Chain | Residue |
| D | MET176 |
| D | CYS181 |
| D | GLU182 |
| D | ASN221 |
| D | CYS223 |
| D | ASN293 |
| D | SF4575 |
| E | HIS33 |
| E | ILE41 |
| E | ARG43 |
| E | ARG55 |
| E | ARG83 |
| E | THR85 |
| E | SER86 |
| E | ARG87 |
| E | ASN89 |
| E | GLY117 |
| E | TRP119 |
| E | ALA121 |
| E | SER129 |
| E | MET170 |
| E | ARG172 |
| E | LYS271 |
| E | LEU272 |
| E | SER273 |
| E | ARG276 |
| E | ARG319 |
Functional Information from PROSITE/UniProt
| site_id | PS00198 |
| Number of Residues | 12 |
| Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CmYCGnCYtMCP |
| Chain | Residue | Details |
| B | CYS241-PRO252 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18495156, ECO:0000269|PubMed:20822098, ECO:0007744|PDB:3MM5, ECO:0007744|PDB:3MMC |
| Chain | Residue | Details |
| B | CYS140 | |
| E | CYS178 | |
| E | CYS220 | |
| E | CYS241 | |
| E | CYS244 | |
| E | CYS247 | |
| B | CYS177 | |
| B | CYS178 | |
| B | CYS220 | |
| B | CYS241 | |
| B | CYS244 | |
| B | CYS247 | |
| E | CYS140 | |
| E | CYS177 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue => ECO:0000305|PubMed:18495156, ECO:0000305|PubMed:20822098 |
| Chain | Residue | Details |
| B | CYS182 | |
| E | CYS182 |
