3SXX
Hansenula polymorpha copper amine oxidase-1 in complex with Co(II)
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 methylamine 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 methylamine 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 methylamine 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 methylamine 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 methylamine 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 methylamine 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 | 7 |
Details | BINDING SITE FOR RESIDUE CO A 801 |
Chain | Residue |
A | TYR405 |
A | LEU425 |
A | HIS456 |
A | HIS458 |
A | HIS624 |
A | HOH1628 |
A | HOH1736 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 802 |
Chain | Residue |
A | VAL215 |
A | GLY435 |
A | ASP436 |
A | ASN450 |
A | HOH1031 |
A | HOH1083 |
A | ARG213 |
A | LYS214 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GOL A 803 |
Chain | Residue |
A | GLU368 |
A | LYS393 |
A | TYR410 |
A | VAL412 |
A | ARG420 |
A | ASP422 |
A | ARG424 |
A | HOH1007 |
A | HOH1431 |
A | HOH1458 |
A | HOH1650 |
B | GLY371 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 804 |
Chain | Residue |
A | ARG61 |
A | ILE65 |
A | ASP471 |
A | ASP613 |
A | HOH1303 |
A | HOH1326 |
A | HOH1589 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 805 |
Chain | Residue |
A | GLN66 |
A | GLN70 |
A | GLY72 |
E | TYR448 |
F | TYR534 |
F | HOH912 |
F | HOH1875 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 806 |
Chain | Residue |
A | PRO484 |
A | TYR485 |
A | TYR499 |
A | HOH1447 |
A | HOH1647 |
B | PRO442 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 807 |
Chain | Residue |
A | HIS23 |
A | TYR64 |
A | LYS68 |
A | VAL258 |
A | LYS265 |
A | PHE266 |
A | ASP280 |
A | HOH920 |
A | HOH1490 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 808 |
Chain | Residue |
A | HIS218 |
A | LYS219 |
A | TYR448 |
A | HOH1630 |
B | TYR534 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 809 |
Chain | Residue |
A | ARG57 |
A | GLU93 |
A | GLY94 |
A | GLU105 |
A | ARG107 |
A | HOH1763 |
A | HOH1765 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 810 |
Chain | Residue |
A | TYR160 |
A | LEU558 |
A | LYS561 |
A | SER591 |
A | HOH1903 |
F | LYS561 |
F | ASP593 |
F | GOL808 |
F | HOH1087 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 811 |
Chain | Residue |
A | GLY142 |
A | PRO144 |
A | GLU147 |
A | TYR177 |
A | LYS217 |
A | HOH1295 |
E | HOH1647 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CO B 801 |
Chain | Residue |
B | TYR405 |
B | LEU425 |
B | HIS456 |
B | HIS458 |
B | HIS624 |
B | HOH1629 |
B | HOH1736 |
site_id | BC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 802 |
Chain | Residue |
B | ARG213 |
B | LYS214 |
B | VAL215 |
B | GLY435 |
B | ASP436 |
B | ASN450 |
B | HOH1025 |
B | HOH1663 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 803 |
Chain | Residue |
B | GLU368 |
B | LYS393 |
B | TYR410 |
B | ASP422 |
B | HOH1005 |
B | HOH1125 |
B | HOH1462 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 804 |
Chain | Residue |
A | PRO442 |
B | PRO484 |
B | TYR485 |
B | TYR499 |
B | HOH1501 |
B | HOH1826 |
site_id | BC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 805 |
Chain | Residue |
B | HIS23 |
B | TYR64 |
B | LYS68 |
B | VAL258 |
B | LYS265 |
B | PHE266 |
B | HIS267 |
B | ASP280 |
B | HOH1211 |
site_id | BC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 806 |
Chain | Residue |
B | HIS218 |
B | LYS219 |
B | HOH1901 |
site_id | BC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL B 807 |
Chain | Residue |
B | TYR160 |
B | LEU558 |
B | LYS561 |
B | SER591 |
B | HOH1484 |
B | HOH1712 |
C | LYS561 |
C | ASP593 |
C | GOL809 |
C | HOH1147 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 808 |
Chain | Residue |
B | GLY142 |
B | PRO144 |
B | GLU147 |
B | TYR177 |
B | HOH1327 |
D | HOH1360 |
site_id | CC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 809 |
Chain | Residue |
B | PHE310 |
B | HOH1069 |
B | HOH1162 |
B | HOH1281 |
B | HOH1395 |
B | HOH1792 |
B | HOH1840 |
C | GLY594 |
C | HOH1160 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CO C 801 |
Chain | Residue |
C | TYR405 |
C | HIS456 |
C | HIS458 |
C | HIS624 |
C | HOH1633 |
C | HOH1731 |
site_id | CC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 802 |
Chain | Residue |
C | ARG213 |
C | LYS214 |
C | VAL215 |
C | GLY435 |
C | ASP436 |
C | HOH1076 |
C | HOH1170 |
site_id | CC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL C 803 |
Chain | Residue |
C | GLU368 |
C | LYS393 |
C | TYR410 |
C | VAL412 |
C | ARG420 |
C | ASP422 |
C | HOH1047 |
C | HOH1767 |
D | GLY371 |
site_id | CC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 C 804 |
Chain | Residue |
C | HIS218 |
C | LYS219 |
C | HOH1497 |
C | HOH1608 |
site_id | CC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 805 |
Chain | Residue |
C | PRO484 |
C | TYR485 |
C | TYR499 |
C | HOH1395 |
C | HOH1662 |
D | PRO442 |
D | TRP443 |
site_id | CC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL C 806 |
Chain | Residue |
C | HIS23 |
C | TYR64 |
C | LYS68 |
C | LYS265 |
C | ASP280 |
C | HOH1067 |
C | HOH1578 |
C | HOH1586 |
site_id | CC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 807 |
Chain | Residue |
B | GLN66 |
B | GLN70 |
B | GLY72 |
C | TYR534 |
C | THR650 |
C | HOH1032 |
C | HOH1265 |
site_id | DC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL C 808 |
Chain | Residue |
B | GLY594 |
B | HOH1154 |
C | ARG163 |
C | PHE310 |
C | HOH1113 |
C | HOH1181 |
C | HOH1274 |
C | HOH1367 |
C | HOH1837 |
site_id | DC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL C 809 |
Chain | Residue |
B | LYS561 |
B | ASP593 |
B | GOL807 |
C | LEU558 |
C | LYS561 |
C | SER591 |
C | HOH1147 |
C | HOH1668 |
site_id | DC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL C 810 |
Chain | Residue |
B | TRP67 |
B | LYS68 |
site_id | DC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CO D 801 |
Chain | Residue |
D | TYR405 |
D | HIS456 |
D | HIS458 |
D | HIS624 |
D | HOH1642 |
D | HOH1745 |
site_id | DC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL D 802 |
Chain | Residue |
D | HIS23 |
D | TYR64 |
D | LYS68 |
D | LYS265 |
D | ASP280 |
D | HOH1167 |
D | HOH1870 |
site_id | DC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GOL D 803 |
Chain | Residue |
D | GLU368 |
D | LYS393 |
D | TYR410 |
D | VAL412 |
D | ARG420 |
D | ASP422 |
D | ARG424 |
D | HOH1051 |
D | HOH1596 |
D | HOH1772 |
D | HOH1934 |
site_id | DC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL D 804 |
Chain | Residue |
D | PRO484 |
D | TYR485 |
D | TYR499 |
D | HOH1586 |
D | HOH1643 |
site_id | DC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL D 805 |
Chain | Residue |
D | SER179 |
D | ASP183 |
D | HIS188 |
D | HIS218 |
D | LYS219 |
D | HIS220 |
D | HOH1313 |
D | HOH1550 |
site_id | DC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL D 806 |
Chain | Residue |
B | HOH1152 |
B | HOH1742 |
C | HOH1101 |
D | HIS218 |
D | LYS219 |
D | TYR448 |
site_id | EC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CO E 801 |
Chain | Residue |
E | TYR405 |
E | HIS456 |
E | HIS458 |
E | HIS624 |
E | HOH1637 |
E | HOH1731 |
site_id | EC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL E 802 |
Chain | Residue |
E | HIS23 |
E | TYR64 |
E | LYS68 |
E | LYS265 |
E | ASP280 |
E | HOH1225 |
E | HOH1368 |
E | HOH1756 |
site_id | EC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL E 803 |
Chain | Residue |
E | GLU368 |
E | LYS393 |
E | TYR410 |
E | VAL412 |
E | ARG420 |
E | ASP422 |
E | ARG424 |
E | HOH922 |
E | HOH1620 |
F | GLY371 |
site_id | EC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL E 804 |
Chain | Residue |
E | PRO484 |
E | TYR485 |
E | HOH1658 |
E | HOH1852 |
site_id | EC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL E 805 |
Chain | Residue |
A | ASN529 |
A | HOH1892 |
E | LYS214 |
E | VAL215 |
E | ASP436 |
E | ASN450 |
E | HOH1050 |
E | HOH1151 |
E | HOH1326 |
site_id | EC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL E 806 |
Chain | Residue |
A | HOH1571 |
A | HOH1688 |
E | HIS218 |
E | LYS219 |
E | TYR448 |
F | HOH1037 |
site_id | EC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CO F 801 |
Chain | Residue |
F | TYR405 |
F | LEU425 |
F | HIS456 |
F | HIS458 |
F | HIS624 |
F | HOH1599 |
F | HOH1705 |
site_id | EC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL F 802 |
Chain | Residue |
F | HIS23 |
F | TYR64 |
F | LYS68 |
F | LYS265 |
F | ASP280 |
F | HOH1093 |
F | HOH1490 |
site_id | EC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL F 803 |
Chain | Residue |
F | ARG213 |
F | LYS214 |
F | VAL215 |
F | GLY435 |
F | ASP436 |
F | HOH1095 |
F | HOH1725 |
site_id | FC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE GOL F 804 |
Chain | Residue |
E | GLY371 |
F | GLU368 |
F | LYS393 |
F | TYR410 |
F | VAL412 |
F | ARG420 |
F | ASP422 |
F | ARG424 |
F | HOH1059 |
F | HOH1133 |
F | HOH1634 |
F | HOH1696 |
F | HOH1703 |
F | HOH1896 |
site_id | FC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL F 805 |
Chain | Residue |
E | PRO442 |
F | PRO484 |
F | TYR485 |
F | TYR499 |
F | HOH1181 |
F | HOH1527 |
site_id | FC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 F 806 |
Chain | Residue |
F | HIS218 |
F | LYS219 |
F | HOH1675 |
F | HOH1887 |
site_id | FC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL F 807 |
Chain | Residue |
A | TRP67 |
A | LYS68 |
site_id | FC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL F 808 |
Chain | Residue |
A | LYS561 |
A | ASP593 |
A | GOL810 |
F | TYR160 |
F | LEU558 |
F | LYS561 |
F | SER591 |
F | HOH1087 |
F | HOH1623 |
site_id | FC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL F 809 |
Chain | Residue |
A | GLY594 |
A | HOH952 |
F | ARG163 |
F | PHE310 |
F | HOH934 |
F | HOH1190 |
F | HOH1204 |
F | HOH1313 |
F | HOH1857 |
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 | TYR405 | |
B | TYR405 | |
C | TYR405 | |
D | TYR405 | |
E | TYR405 | |
F | TYR405 |
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 | TYR405 | |
B | TYR405 | |
C | TYR405 | |
D | TYR405 | |
E | TYR405 | |
F | TYR405 |
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 |