4KFD
Crystal structure of Hansenula polymorpha copper amine oxidase-1 reduced by methylamine at pH 6.0
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005777 | cellular_component | peroxisome |
| A | 0008131 | molecular_function | primary amine oxidase activity |
| A | 0009308 | biological_process | amine metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048038 | molecular_function | quinone binding |
| A | 0052595 | molecular_function | aliphatic amine oxidase activity |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005777 | cellular_component | peroxisome |
| B | 0008131 | molecular_function | primary amine oxidase activity |
| B | 0009308 | biological_process | amine metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048038 | molecular_function | quinone binding |
| B | 0052595 | molecular_function | aliphatic amine oxidase activity |
| C | 0005507 | molecular_function | copper ion binding |
| C | 0005777 | cellular_component | peroxisome |
| C | 0008131 | molecular_function | primary amine oxidase activity |
| C | 0009308 | biological_process | amine metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0048038 | molecular_function | quinone binding |
| C | 0052595 | molecular_function | aliphatic amine oxidase activity |
| D | 0005507 | molecular_function | copper ion binding |
| D | 0005777 | cellular_component | peroxisome |
| D | 0008131 | molecular_function | primary amine oxidase activity |
| D | 0009308 | biological_process | amine metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0048038 | molecular_function | quinone binding |
| D | 0052595 | molecular_function | aliphatic amine oxidase activity |
| E | 0005507 | molecular_function | copper ion binding |
| E | 0005777 | cellular_component | peroxisome |
| E | 0008131 | molecular_function | primary amine oxidase activity |
| E | 0009308 | biological_process | amine metabolic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0048038 | molecular_function | quinone binding |
| E | 0052595 | molecular_function | aliphatic amine oxidase activity |
| F | 0005507 | molecular_function | copper ion binding |
| F | 0005777 | cellular_component | peroxisome |
| F | 0008131 | molecular_function | primary amine oxidase activity |
| F | 0009308 | biological_process | amine metabolic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0048038 | molecular_function | quinone binding |
| F | 0052595 | molecular_function | aliphatic amine oxidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU A 801 |
| Chain | Residue |
| A | HIS456 |
| A | HIS458 |
| A | HIS624 |
| A | PEO802 |
| A | HOH1428 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEO A 802 |
| Chain | Residue |
| A | CU801 |
| A | HOH1052 |
| A | HOH1428 |
| A | TYY405 |
| A | HIS456 |
| A | HIS624 |
| A | MET634 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 803 |
| Chain | Residue |
| A | GLN66 |
| A | GLN70 |
| A | GLY72 |
| A | HOH954 |
| A | HOH1348 |
| F | TYR534 |
| F | THR650 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 804 |
| Chain | Residue |
| A | LYS214 |
| A | VAL215 |
| A | GLY435 |
| A | ASP436 |
| A | HOH1131 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 805 |
| Chain | Residue |
| A | GLU368 |
| A | LYS393 |
| A | VAL412 |
| A | ASP422 |
| A | HOH1069 |
| A | HOH1561 |
| A | HOH1579 |
| B | GLY371 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 806 |
| Chain | Residue |
| A | PRO484 |
| A | HOH1690 |
| B | PRO442 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 807 |
| Chain | Residue |
| A | HIS218 |
| A | LYS219 |
| A | TYR448 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 808 |
| Chain | Residue |
| A | LYS561 |
| A | SER591 |
| A | HOH1245 |
| F | LYS561 |
| F | ASP593 |
| F | GOL811 |
| F | HOH996 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 809 |
| Chain | Residue |
| A | TRP67 |
| A | LYS68 |
| F | HOH1636 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 810 |
| Chain | Residue |
| A | GLY142 |
| A | PRO144 |
| A | GLU147 |
| A | TYR177 |
| A | HOH1678 |
| E | HOH1355 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 811 |
| Chain | Residue |
| A | ARG61 |
| A | LYS62 |
| A | ILE65 |
| A | ASP471 |
| A | ASP613 |
| A | HOH1323 |
| A | HOH1533 |
| A | HOH1663 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 812 |
| Chain | Residue |
| A | ASP131 |
| A | VAL203 |
| A | ILE204 |
| A | HOH1495 |
| A | HOH1698 |
| F | GLU110 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 813 |
| Chain | Residue |
| A | PRO59 |
| A | ARG61 |
| A | HIS294 |
| A | TYR575 |
| A | ASN578 |
| A | HOH911 |
| A | HOH1139 |
| A | HOH1302 |
| A | HOH1407 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 814 |
| Chain | Residue |
| A | SER251 |
| A | LYS253 |
| A | GLU260 |
| A | HOH1191 |
| A | HOH1255 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 801 |
| Chain | Residue |
| B | HIS456 |
| B | HIS458 |
| B | HIS624 |
| B | PEO802 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEO B 802 |
| Chain | Residue |
| B | TYY405 |
| B | LEU429 |
| B | HIS456 |
| B | HIS458 |
| B | HIS624 |
| B | MET634 |
| B | CU801 |
| B | HOH1096 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 803 |
| Chain | Residue |
| B | ASP422 |
| B | HOH1031 |
| B | HOH1527 |
| A | GLY371 |
| B | GLU368 |
| B | LYS393 |
| B | VAL412 |
| B | ARG420 |
| site_id | BC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 804 |
| Chain | Residue |
| B | PRO59 |
| B | ALA60 |
| B | ARG61 |
| B | HIS294 |
| B | TYR575 |
| B | ASN578 |
| B | HOH908 |
| B | HOH1039 |
| B | HOH1051 |
| B | HOH1287 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 805 |
| Chain | Residue |
| A | PRO442 |
| B | PRO484 |
| B | TYR499 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 806 |
| Chain | Residue |
| A | TYR534 |
| B | HIS218 |
| B | LYS219 |
| B | TYR448 |
| B | PO4810 |
| B | HOH1636 |
| site_id | CC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 807 |
| Chain | Residue |
| B | LYS561 |
| B | SER591 |
| B | HOH990 |
| B | HOH1399 |
| C | LYS561 |
| C | ASP593 |
| C | GOL811 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 808 |
| Chain | Residue |
| B | ARG61 |
| B | ASP613 |
| B | HOH1516 |
| B | HOH1635 |
| D | HOH1396 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 809 |
| Chain | Residue |
| B | LYS214 |
| B | VAL215 |
| B | ASP436 |
| B | ASN450 |
| B | HOH1023 |
| B | HOH1659 |
| site_id | CC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 B 810 |
| Chain | Residue |
| B | HIS218 |
| B | LYS219 |
| B | GOL806 |
| site_id | CC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 811 |
| Chain | Residue |
| B | GLY142 |
| B | PRO144 |
| B | GLU147 |
| B | TYR177 |
| B | VAL215 |
| B | HOH1147 |
| D | HOH1545 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU C 801 |
| Chain | Residue |
| C | HIS456 |
| C | HIS458 |
| C | HIS624 |
| C | PEO802 |
| C | HOH1427 |
| site_id | CC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEO C 802 |
| Chain | Residue |
| C | TYY405 |
| C | HIS456 |
| C | HIS458 |
| C | HIS624 |
| C | MET634 |
| C | CU801 |
| C | HOH990 |
| C | HOH1427 |
| site_id | DC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 803 |
| Chain | Residue |
| C | HIS23 |
| C | TYR64 |
| C | LYS68 |
| C | LYS265 |
| C | ASP280 |
| C | HOH965 |
| C | HOH1543 |
| site_id | DC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 804 |
| Chain | Residue |
| C | LYS214 |
| C | VAL215 |
| C | GLY435 |
| C | ASP436 |
| C | HOH1252 |
| site_id | DC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL C 805 |
| Chain | Residue |
| B | LYS68 |
| C | HOH1556 |
| site_id | DC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 806 |
| Chain | Residue |
| C | GLU368 |
| C | LYS393 |
| C | VAL412 |
| C | ARG420 |
| C | ASP422 |
| C | HOH1034 |
| C | HOH1590 |
| D | GLY371 |
| site_id | DC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 807 |
| Chain | Residue |
| C | PRO484 |
| C | TYR499 |
| D | PRO442 |
| site_id | DC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 C 808 |
| Chain | Residue |
| C | HIS218 |
| C | LYS219 |
| site_id | DC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL C 809 |
| Chain | Residue |
| B | GLN66 |
| B | GLN70 |
| B | GLY72 |
| C | TYR534 |
| C | THR650 |
| C | GLU651 |
| C | HOH942 |
| C | HOH1509 |
| D | LYS231 |
| site_id | DC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL C 810 |
| Chain | Residue |
| C | ARG57 |
| C | TYR80 |
| C | ASN578 |
| C | TYR581 |
| C | ASP585 |
| C | HOH1146 |
| C | HOH1257 |
| C | HOH1361 |
| C | HOH1412 |
| C | HOH1516 |
| site_id | DC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 811 |
| Chain | Residue |
| B | LYS561 |
| B | ASP593 |
| B | GOL807 |
| B | HOH990 |
| C | TYR160 |
| C | LYS561 |
| C | SER591 |
| C | HOH1535 |
| site_id | EC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU D 801 |
| Chain | Residue |
| D | HIS456 |
| D | HIS458 |
| D | HIS624 |
| D | PEO802 |
| D | HOH1473 |
| site_id | EC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEO D 802 |
| Chain | Residue |
| D | TYY405 |
| D | HIS456 |
| D | HIS458 |
| D | HIS624 |
| D | MET634 |
| D | CU801 |
| D | HOH905 |
| site_id | EC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL D 803 |
| Chain | Residue |
| D | GLY142 |
| D | PRO144 |
| D | GLU147 |
| D | TYR177 |
| D | LYS217 |
| D | GOL804 |
| D | HOH1226 |
| D | HOH1608 |
| site_id | EC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 804 |
| Chain | Residue |
| D | LYS150 |
| D | TYR177 |
| D | GOL803 |
| D | HOH1322 |
| D | HOH1529 |
| site_id | EC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL D 806 |
| Chain | Residue |
| B | LYS62 |
| B | ALA63 |
| B | GLN66 |
| B | PRO73 |
| B | HOH1010 |
| B | HOH1348 |
| B | HOH1625 |
| D | LYS231 |
| D | VAL232 |
| D | GLY233 |
| site_id | EC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL D 807 |
| Chain | Residue |
| C | GLY371 |
| D | GLU368 |
| D | LYS393 |
| D | VAL412 |
| D | ARG420 |
| D | ASP422 |
| D | ARG424 |
| D | HOH1095 |
| D | HOH1275 |
| D | HOH1541 |
| D | HOH1570 |
| site_id | EC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL D 808 |
| Chain | Residue |
| D | PRO18 |
| D | ALA19 |
| D | ALA99 |
| site_id | EC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 809 |
| Chain | Residue |
| D | HIS23 |
| D | TYR64 |
| D | LYS68 |
| D | LYS265 |
| D | ASP280 |
| D | HOH1006 |
| site_id | EC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL D 810 |
| Chain | Residue |
| D | TRP67 |
| D | LYS68 |
| site_id | FC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 811 |
| Chain | Residue |
| D | LEU56 |
| D | ARG57 |
| D | TYR80 |
| D | LEU580 |
| D | HOH1090 |
| D | HOH1187 |
| D | HOH1634 |
| site_id | FC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU E 801 |
| Chain | Residue |
| E | HIS456 |
| E | HIS458 |
| E | HIS624 |
| E | PEO802 |
| E | HOH1439 |
| site_id | FC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEO E 802 |
| Chain | Residue |
| E | TYY405 |
| E | HIS456 |
| E | HIS458 |
| E | HIS624 |
| E | MET634 |
| E | CU801 |
| E | HOH903 |
| E | HOH1439 |
| site_id | FC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL E 803 |
| Chain | Residue |
| E | GLY142 |
| E | PRO144 |
| E | GLU147 |
| E | TYR177 |
| E | LYS217 |
| E | HOH1249 |
| site_id | FC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL E 804 |
| Chain | Residue |
| E | PHE252 |
| E | LYS253 |
| E | MET254 |
| E | ILE342 |
| E | HIS343 |
| E | HOH1507 |
| E | HOH1656 |
| site_id | FC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL E 805 |
| Chain | Residue |
| E | GLU58 |
| E | PRO59 |
| E | TYR575 |
| E | ASP577 |
| E | ASN578 |
| E | HOH947 |
| E | HOH1524 |
| site_id | FC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL E 806 |
| Chain | Residue |
| E | PRO484 |
| F | PRO442 |
| site_id | FC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL E 807 |
| Chain | Residue |
| E | HIS23 |
| E | TYR64 |
| E | LYS68 |
| E | LYS265 |
| E | ASP280 |
| E | HOH975 |
| site_id | FC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL E 808 |
| Chain | Residue |
| E | GLU368 |
| E | LYS393 |
| E | ARG420 |
| E | ASP422 |
| E | ARG424 |
| E | HOH1036 |
| E | HOH1307 |
| E | HOH1450 |
| F | GLY371 |
| site_id | GC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU F 801 |
| Chain | Residue |
| F | HIS456 |
| F | HIS458 |
| F | HIS624 |
| F | PEO802 |
| F | HOH1402 |
| site_id | GC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEO F 802 |
| Chain | Residue |
| F | TYY405 |
| F | LEU429 |
| F | HIS456 |
| F | HIS458 |
| F | HIS624 |
| F | MET634 |
| F | CU801 |
| F | HOH986 |
| site_id | GC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL F 803 |
| Chain | Residue |
| F | HIS23 |
| F | TYR64 |
| F | LYS68 |
| F | LYS265 |
| F | ASP280 |
| F | HOH948 |
| F | HOH1470 |
| site_id | GC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL F 804 |
| Chain | Residue |
| E | GLY371 |
| F | LYS393 |
| F | VAL412 |
| F | ARG420 |
| F | ASP422 |
| F | GOL805 |
| F | HOH1039 |
| site_id | GC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL F 805 |
| Chain | Residue |
| E | GLY371 |
| E | ARG390 |
| F | ASP337 |
| F | CYS338 |
| F | LYS339 |
| F | GLU368 |
| F | GOL804 |
| F | HOH1338 |
| site_id | GC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL F 806 |
| Chain | Residue |
| F | PHE252 |
| F | LYS253 |
| F | MET254 |
| F | HIS343 |
| F | HOH1202 |
| F | HOH1530 |
| site_id | GC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL F 807 |
| Chain | Residue |
| F | PRO484 |
| F | TYR485 |
| F | TYR499 |
| site_id | GC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 F 808 |
| Chain | Residue |
| F | HIS218 |
| F | LYS219 |
| site_id | GC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL F 809 |
| Chain | Residue |
| F | LEU512 |
| F | ASP604 |
| F | GLY605 |
| F | HOH1072 |
| F | HOH1382 |
| F | HOH1566 |
| F | HOH1628 |
| site_id | HC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL F 810 |
| Chain | Residue |
| A | GLU110 |
| F | ALA133 |
| F | VAL203 |
| F | ILE204 |
| F | HOH1113 |
| F | HOH1409 |
| F | HOH1477 |
| F | HOH1629 |
| site_id | HC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL F 811 |
| Chain | Residue |
| A | LYS561 |
| A | ASP593 |
| A | GOL808 |
| F | TYR160 |
| F | LYS561 |
| F | SER591 |
| F | HOH996 |
| F | HOH1517 |
| site_id | HC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL F 812 |
| Chain | Residue |
| F | GLU58 |
| F | PRO59 |
| F | ARG61 |
| F | TYR575 |
| F | ASP577 |
| F | ASN578 |
| F | HOH925 |
| F | HOH990 |
| F | HOH1181 |
| F | HOH1214 |
Functional Information from PROSITE/UniProt
| site_id | PS01159 |
| Number of Residues | 26 |
| Details | WW_DOMAIN_1 WW/rsp5/WWP domain signature. WgtgkrlqqalvYYrsdedd.SQYSHP |
| Chain | Residue | Details |
| A | TRP164-PRO189 |
| site_id | PS01164 |
| Number of Residues | 14 |
| Details | COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVVsqifTaaNYEY |
| Chain | Residue | Details |
| A | LEU394-TYR407 |
| site_id | PS01165 |
| Number of Residues | 14 |
| Details | COPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TfGitHFpapEDfP |
| Chain | Residue | Details |
| A | THR619-PRO632 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:9551552 |
| Chain | Residue | Details |
| A | ASP319 | |
| B | ASP319 | |
| C | ASP319 | |
| D | ASP319 | |
| E | ASP319 | |
| F | ASP319 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | ACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4KFF |
| Chain | Residue | Details |
| A | TYY405 | |
| B | TYY405 | |
| C | TYY405 | |
| D | TYY405 | |
| E | TYY405 | |
| F | TYY405 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5 |
| Chain | Residue | Details |
| A | ALA317 | |
| B | ALA317 | |
| C | ALA317 | |
| D | ALA317 | |
| E | ALA317 | |
| F | ALA317 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P46883 |
| Chain | Residue | Details |
| A | ALA402 | |
| B | ALA402 | |
| C | ALA402 | |
| D | ALA402 | |
| E | ALA402 | |
| F | ALA402 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV, ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD, ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF |
| Chain | Residue | Details |
| A | HIS456 | |
| D | HIS456 | |
| D | HIS458 | |
| D | HIS624 | |
| E | HIS456 | |
| E | HIS458 | |
| E | HIS624 | |
| F | HIS456 | |
| F | HIS458 | |
| F | HIS624 | |
| A | HIS458 | |
| A | HIS624 | |
| B | HIS456 | |
| B | HIS458 | |
| B | HIS624 | |
| C | HIS456 | |
| C | HIS458 | |
| C | HIS624 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q43077 |
| Chain | Residue | Details |
| A | ASP465 | |
| D | ASP465 | |
| D | ASP613 | |
| D | ILE614 | |
| E | ASP465 | |
| E | ASP613 | |
| E | ILE614 | |
| F | ASP465 | |
| F | ASP613 | |
| F | ILE614 | |
| A | ASP613 | |
| A | ILE614 | |
| B | ASP465 | |
| B | ASP613 | |
| B | ILE614 | |
| C | ASP465 | |
| C | ASP613 | |
| C | ILE614 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | MOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:2OQE |
| Chain | Residue | Details |
| A | TYY405 | |
| B | TYY405 | |
| C | TYY405 | |
| D | TYY405 | |
| E | TYY405 | |
| F | TYY405 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:9551552 |
| Chain | Residue | Details |
| A | ASN243 | |
| B | ASN243 | |
| C | ASN243 | |
| D | ASN243 | |
| E | ASN243 | |
| F | ASN243 |
