6CZ9
The arsenate respiratory reductase (Arr) complex from Shewanella sp. ANA-3 bound to arsenite
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030611 | molecular_function | arsenate reductase activity |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0043546 | molecular_function | molybdopterin cofactor 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 | 0042597 | cellular_component | periplasmic space |
| 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 |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0030611 | molecular_function | arsenate reductase activity |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0043546 | molecular_function | molybdopterin cofactor binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| D | 0042597 | cellular_component | periplasmic space |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue SF4 A 901 |
| Chain | Residue |
| A | CYS61 |
| A | ARG98 |
| A | SER236 |
| A | GLY63 |
| A | CYS64 |
| A | SER66 |
| A | TRP67 |
| A | CYS68 |
| A | LYS70 |
| A | SER95 |
| A | CYS96 |
| site_id | AC2 |
| Number of Residues | 35 |
| Details | binding site for residue MGD A 902 |
| Chain | Residue |
| A | CYS64 |
| A | ARG98 |
| A | ARG165 |
| A | CYS193 |
| A | PHE224 |
| A | GLY225 |
| A | ALA230 |
| A | SER231 |
| A | ASN232 |
| A | VAL254 |
| A | ASP255 |
| A | PRO256 |
| A | ARG257 |
| A | PRO273 |
| A | GLY274 |
| A | ASP276 |
| A | SER373 |
| A | ARG374 |
| A | GLY375 |
| A | GLN379 |
| A | VAL721 |
| A | ASP722 |
| A | LYS724 |
| A | SER725 |
| A | ARG726 |
| A | ASN728 |
| A | GLU730 |
| A | TYR844 |
| A | MGD903 |
| A | MO904 |
| A | AST905 |
| A | HOH1075 |
| A | HOH1155 |
| A | HOH1264 |
| A | HOH1294 |
| site_id | AC3 |
| Number of Residues | 36 |
| Details | binding site for residue MGD A 903 |
| Chain | Residue |
| A | GLY164 |
| A | ARG165 |
| A | HIS189 |
| A | VAL192 |
| A | CYS193 |
| A | ARG374 |
| A | PHE481 |
| A | ASN482 |
| A | ASN483 |
| A | PHE484 |
| A | SER487 |
| A | ILE507 |
| A | THR508 |
| A | THR509 |
| A | SER512 |
| A | SER524 |
| A | HIS526 |
| A | HIS527 |
| A | ASP561 |
| A | ASP722 |
| A | LYS724 |
| A | GLU730 |
| A | GLY731 |
| A | ARG732 |
| A | PHE802 |
| A | TYR809 |
| A | ASN827 |
| A | PHE843 |
| A | MGD902 |
| A | MO904 |
| A | AST905 |
| A | HOH1050 |
| A | HOH1061 |
| A | HOH1100 |
| A | HOH1111 |
| A | HOH1284 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MO A 904 |
| Chain | Residue |
| A | CYS193 |
| A | MGD902 |
| A | MGD903 |
| A | AST905 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue AST A 905 |
| Chain | Residue |
| A | ARG165 |
| A | TYR166 |
| A | HIS189 |
| A | CYS193 |
| A | TYR210 |
| A | MGD902 |
| A | MGD903 |
| A | MO904 |
| A | HOH1051 |
| A | HOH1330 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue FMT A 906 |
| Chain | Residue |
| A | HOH1229 |
| A | HOH1426 |
| A | TYR645 |
| A | LYS646 |
| A | ALA649 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue FMT A 907 |
| Chain | Residue |
| A | GLN62 |
| A | GLY63 |
| A | GLN105 |
| A | HIS527 |
| A | LYS729 |
| A | ARG732 |
| A | HOH1050 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue FMT A 908 |
| Chain | Residue |
| A | ARG50 |
| A | ASP76 |
| B | GLU215 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue FMT A 909 |
| Chain | Residue |
| A | GLU753 |
| A | ASP754 |
| A | GLY823 |
| A | HOH1104 |
| A | HOH1269 |
| D | ASN97 |
| D | HOH447 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue PG5 A 910 |
| Chain | Residue |
| A | ARG794 |
| A | PRO795 |
| A | HOH1005 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 B 301 |
| Chain | Residue |
| B | CYS12 |
| B | VAL13 |
| B | CYS15 |
| B | GLY16 |
| B | CYS18 |
| B | TYR52 |
| B | CYS183 |
| B | ARG188 |
| site_id | AD3 |
| Number of Residues | 10 |
| Details | binding site for residue SF4 B 302 |
| Chain | Residue |
| B | CYS22 |
| B | ASN26 |
| B | TRP34 |
| B | SER35 |
| B | CYS164 |
| B | THR165 |
| B | PHE166 |
| B | CYS167 |
| B | PRO177 |
| B | CYS179 |
| site_id | AD4 |
| Number of Residues | 10 |
| Details | binding site for residue SF4 B 303 |
| Chain | Residue |
| B | CYS57 |
| B | ASN58 |
| B | CYS60 |
| B | PRO64 |
| B | CYS65 |
| B | THR82 |
| B | CYS99 |
| B | TYR101 |
| B | ILE104 |
| B | LYS163 |
| site_id | AD5 |
| Number of Residues | 9 |
| Details | binding site for residue SF4 B 304 |
| Chain | Residue |
| B | CYS69 |
| B | THR71 |
| B | GLN84 |
| B | CYS89 |
| B | ILE90 |
| B | CYS92 |
| B | LYS93 |
| B | CYS95 |
| B | THR161 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue FMT B 305 |
| Chain | Residue |
| B | ARG2 |
| B | LEU193 |
| B | HOH411 |
| B | HOH448 |
| site_id | AD7 |
| Number of Residues | 12 |
| Details | binding site for residue SF4 C 901 |
| Chain | Residue |
| C | CYS61 |
| C | GLY63 |
| C | CYS64 |
| C | SER66 |
| C | TRP67 |
| C | CYS68 |
| C | LYS70 |
| C | SER95 |
| C | CYS96 |
| C | ARG98 |
| C | VAL235 |
| C | SER236 |
| site_id | AD8 |
| Number of Residues | 37 |
| Details | binding site for residue MGD C 902 |
| Chain | Residue |
| C | CYS64 |
| C | THR65 |
| C | ARG98 |
| C | ARG165 |
| C | CYS193 |
| C | PHE224 |
| C | GLY225 |
| C | ALA230 |
| C | SER231 |
| C | ASN232 |
| C | VAL254 |
| C | ASP255 |
| C | PRO256 |
| C | ARG257 |
| C | PRO273 |
| C | GLY274 |
| C | ASP276 |
| C | SER373 |
| C | ARG374 |
| C | GLY375 |
| C | GLN379 |
| C | VAL721 |
| C | ASP722 |
| C | LYS724 |
| C | SER725 |
| C | ARG726 |
| C | ASN728 |
| C | GLU730 |
| C | TYR844 |
| C | MGD903 |
| C | MO904 |
| C | AST905 |
| C | HOH1087 |
| C | HOH1098 |
| C | HOH1189 |
| C | HOH1201 |
| C | HOH1480 |
| site_id | AD9 |
| Number of Residues | 36 |
| Details | binding site for residue MGD C 903 |
| Chain | Residue |
| C | GLY164 |
| C | ARG165 |
| C | HIS189 |
| C | VAL192 |
| C | CYS193 |
| C | ARG374 |
| C | PHE481 |
| C | ASN482 |
| C | ASN483 |
| C | PHE484 |
| C | SER487 |
| C | ILE507 |
| C | THR508 |
| C | THR509 |
| C | SER512 |
| C | SER524 |
| C | HIS527 |
| C | ASP561 |
| C | ASP722 |
| C | LYS724 |
| C | GLU730 |
| C | GLY731 |
| C | ARG732 |
| C | PHE802 |
| C | TYR809 |
| C | ASN827 |
| C | PHE843 |
| C | MGD902 |
| C | MO904 |
| C | AST905 |
| C | HOH1156 |
| C | HOH1183 |
| C | HOH1308 |
| C | HOH1310 |
| C | HOH1316 |
| C | HOH1497 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue MO C 904 |
| Chain | Residue |
| C | CYS193 |
| C | MGD902 |
| C | MGD903 |
| C | AST905 |
| site_id | AE2 |
| Number of Residues | 12 |
| Details | binding site for residue AST C 905 |
| Chain | Residue |
| C | THR65 |
| C | ARG165 |
| C | TYR166 |
| C | HIS189 |
| C | CYS193 |
| C | TYR210 |
| C | MGD902 |
| C | MGD903 |
| C | MO904 |
| C | HOH1041 |
| C | HOH1146 |
| C | HOH1594 |
| site_id | AE3 |
| Number of Residues | 6 |
| Details | binding site for residue FMT C 906 |
| Chain | Residue |
| C | PRO737 |
| C | TYR740 |
| C | ARG822 |
| C | HOH1076 |
| C | HOH1171 |
| C | HOH1623 |
| site_id | AE4 |
| Number of Residues | 5 |
| Details | binding site for residue FMT C 907 |
| Chain | Residue |
| C | GLN105 |
| C | HIS527 |
| C | LYS729 |
| C | ARG732 |
| C | HOH1037 |
| site_id | AE5 |
| Number of Residues | 6 |
| Details | binding site for residue FMT C 908 |
| Chain | Residue |
| C | TYR645 |
| C | LYS646 |
| C | ALA649 |
| C | HOH1094 |
| C | HOH1282 |
| C | HOH1335 |
| site_id | AE6 |
| Number of Residues | 4 |
| Details | binding site for residue PG5 C 909 |
| Chain | Residue |
| C | GLU272 |
| C | ILE346 |
| C | ARG794 |
| C | PRO795 |
| site_id | AE7 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 D 301 |
| Chain | Residue |
| D | CYS12 |
| D | VAL13 |
| D | CYS15 |
| D | GLY16 |
| D | CYS18 |
| D | TYR52 |
| D | CYS183 |
| D | ARG188 |
| site_id | AE8 |
| Number of Residues | 10 |
| Details | binding site for residue SF4 D 302 |
| Chain | Residue |
| D | CYS22 |
| D | ASN26 |
| D | TRP34 |
| D | SER35 |
| D | CYS164 |
| D | THR165 |
| D | PHE166 |
| D | CYS167 |
| D | PRO177 |
| D | CYS179 |
| site_id | AE9 |
| Number of Residues | 10 |
| Details | binding site for residue SF4 D 303 |
| Chain | Residue |
| D | CYS57 |
| D | ASN58 |
| D | CYS60 |
| D | PRO64 |
| D | CYS65 |
| D | THR82 |
| D | CYS99 |
| D | TYR101 |
| D | ILE104 |
| D | LYS163 |
| site_id | AF1 |
| Number of Residues | 9 |
| Details | binding site for residue SF4 D 304 |
| Chain | Residue |
| D | CYS69 |
| D | THR71 |
| D | GLN84 |
| D | CYS89 |
| D | ILE90 |
| D | CYS92 |
| D | LYS93 |
| D | CYS95 |
| D | THR161 |
| site_id | AF2 |
| Number of Residues | 4 |
| Details | binding site for residue PEG D 305 |
| Chain | Residue |
| B | ARG113 |
| D | PRO70 |
| D | HOH403 |
| D | HOH589 |
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. CiGCKkCMnACP |
| Chain | Residue | Details |
| B | CYS89-PRO100 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 112 |
| Details | Domain: {"description":"4Fe-4S Mo/W bis-MGD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01004","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 42 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30104376","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6CZ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CZ8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CZ9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CZA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30104376","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6CZ9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30104376","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6CZ8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 58 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 62 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 58 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






