2OOV
Crystal Structure of Hansenula polymorpha amine oxidase to 1.7 Angstroms
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 | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 801 |
| Chain | Residue |
| A | HIS456 |
| A | HIS458 |
| A | HIS624 |
| A | HOH6215 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 801 |
| Chain | Residue |
| B | HIS456 |
| B | HIS458 |
| B | HIS624 |
| B | HOH6210 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU C 801 |
| Chain | Residue |
| C | HIS456 |
| C | HIS458 |
| C | HIS624 |
| C | TPQ405 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CU D 801 |
| Chain | Residue |
| D | TPQ405 |
| D | LEU425 |
| D | HIS456 |
| D | HIS458 |
| D | HIS624 |
| D | HOH6751 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU E 801 |
| Chain | Residue |
| E | TPQ405 |
| E | HIS456 |
| E | HIS458 |
| E | HIS624 |
| E | HOH6752 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU F 801 |
| Chain | Residue |
| F | TPQ405 |
| F | HIS456 |
| F | HIS458 |
| F | HIS624 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 C 6010 |
| Chain | Residue |
| C | HIS218 |
| C | LYS219 |
| C | HOH6697 |
| C | HOH6762 |
| C | HOH6767 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 F 6011 |
| Chain | Residue |
| F | HIS218 |
| F | LYS219 |
| F | HOH6701 |
| F | HOH6717 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL F 6001 |
| Chain | Residue |
| F | HIS23 |
| F | TYR64 |
| F | LYS68 |
| F | LYS265 |
| F | ASP280 |
| F | HOH6166 |
| F | HOH6746 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 6002 |
| Chain | Residue |
| C | LYS214 |
| C | VAL215 |
| C | ASP436 |
| C | HOH6215 |
| C | HOH6429 |
| C | HOH6812 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL F 6003 |
| Chain | Residue |
| F | PHE51 |
| F | ASN52 |
| F | THR117 |
| F | GLU119 |
| F | ASP120 |
| F | TYR327 |
| F | SER350 |
| F | ASP351 |
| F | ARG352 |
| F | HOH6198 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 6004 |
| Chain | Residue |
| B | ARG213 |
| B | LYS214 |
| B | VAL215 |
| B | ASP436 |
| B | ASN450 |
| B | HOH6581 |
| B | HOH6758 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 6005 |
| Chain | Residue |
| A | LYS214 |
| A | VAL215 |
| A | ASP436 |
| A | HOH6370 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL F 6006 |
| Chain | Residue |
| F | LYS214 |
| F | VAL215 |
| F | GLY435 |
| F | ASP436 |
| F | HOH6453 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 6007 |
| Chain | Residue |
| C | LYS393 |
| C | VAL412 |
| C | ASP422 |
| C | ARG424 |
| C | HOH6164 |
| C | HOH6785 |
| C | HOH6873 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL F 6008 |
| Chain | Residue |
| E | GLY371 |
| F | LYS393 |
| F | ASP422 |
| F | ARG424 |
| F | HOH6112 |
| F | HOH6644 |
| F | HOH6687 |
| site_id | BC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL B 6009 |
| Chain | Residue |
| B | HOH6774 |
| A | GLY371 |
| B | GLU368 |
| B | LYS393 |
| B | TYR410 |
| B | ARG420 |
| B | ASP422 |
| B | ARG424 |
| B | HOH6156 |
| B | HOH6507 |
| B | HOH6677 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 6012 |
| Chain | Residue |
| A | GLU368 |
| A | LYS393 |
| A | VAL412 |
| A | ARG420 |
| A | ASP422 |
| A | HOH6118 |
| A | HOH6557 |
| A | HOH6789 |
| B | GLY371 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 6013 |
| Chain | Residue |
| A | ARG61 |
| A | LYS62 |
| A | ASP471 |
| A | ASP613 |
| A | HOH6623 |
| A | HOH6707 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL E 6014 |
| Chain | Residue |
| E | LYS214 |
| E | VAL215 |
| E | ASP436 |
| E | HOH6235 |
| E | HOH6791 |
| E | HOH6792 |
| E | HOH6793 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL E 6015 |
| Chain | Residue |
| A | ASP471 |
| A | HOH6707 |
| E | HIS218 |
| E | LYS219 |
| E | TYR448 |
| E | HOH6415 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL E 6016 |
| Chain | Residue |
| E | PRO442 |
| E | TRP443 |
| F | PRO484 |
| F | TYR499 |
| site_id | CC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 6017 |
| Chain | Residue |
| A | ARG163 |
| A | PHE310 |
| A | HOH6315 |
| A | HOH6442 |
| A | HOH6632 |
| A | HOH6844 |
| B | HOH6144 |
| F | ASP593 |
| F | GLY594 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 6018 |
| Chain | Residue |
| A | HIS218 |
| A | LYS219 |
| A | TYR448 |
| A | HOH6471 |
| site_id | CC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL E 6019 |
| Chain | Residue |
| E | LYS393 |
| E | VAL412 |
| E | ARG420 |
| E | ASP422 |
| E | ARG424 |
| E | HOH6067 |
| E | HOH6621 |
| E | HOH6664 |
| E | HOH6713 |
| F | GLY371 |
| site_id | CC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL E 6020 |
| Chain | Residue |
| E | PRO484 |
| F | PRO442 |
| site_id | CC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL C 6021 |
| Chain | Residue |
| C | HIS286 |
| C | PHE649 |
| C | THR650 |
| C | GLU651 |
| C | PRO653 |
| C | GOL6029 |
| C | HOH6125 |
| C | HOH6181 |
| C | HOH6294 |
| C | HOH6530 |
| site_id | DC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL E 6022 |
| Chain | Residue |
| E | ILE208 |
| E | PRO209 |
| E | ASN210 |
| E | PHE310 |
| E | HOH6131 |
| E | HOH6282 |
| E | HOH6674 |
| site_id | DC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 6023 |
| Chain | Residue |
| B | GLY142 |
| B | PRO144 |
| B | GLU147 |
| B | TYR177 |
| B | HOH6704 |
| D | HOH6484 |
| site_id | DC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 6024 |
| Chain | Residue |
| B | PRO484 |
| B | TYR499 |
| B | HOH6808 |
| site_id | DC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 6025 |
| Chain | Residue |
| B | GLY603 |
| B | ASP604 |
| B | HOH6375 |
| B | HOH6599 |
| D | PRO490 |
| D | GLU491 |
| site_id | DC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 6026 |
| Chain | Residue |
| B | HIS218 |
| B | LYS219 |
| B | TYR448 |
| B | HOH6275 |
| B | HOH6757 |
| site_id | DC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 6027 |
| Chain | Residue |
| A | PRO484 |
| A | TYR485 |
| A | TYR499 |
| A | HOH6829 |
| A | HOH6862 |
| B | PRO442 |
| site_id | DC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 6028 |
| Chain | Residue |
| D | ARG20 |
| D | PRO21 |
| D | LEU74 |
| D | PRO75 |
| D | ARG77 |
| D | HOH6304 |
| D | HOH6372 |
| D | HOH6662 |
| D | HOH6867 |
| site_id | DC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL C 6029 |
| Chain | Residue |
| B | GLN66 |
| B | GLN70 |
| B | GLY72 |
| C | TYR534 |
| C | THR650 |
| C | GLU651 |
| C | GOL6021 |
| C | HOH6076 |
| C | HOH6530 |
| D | TYR448 |
| site_id | DC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL D 6030 |
| Chain | Residue |
| C | GLY371 |
| D | LYS393 |
| D | VAL412 |
| D | ARG420 |
| D | ASP422 |
| D | ARG424 |
| D | HOH6088 |
| D | HOH6516 |
| D | HOH6744 |
| D | HOH6769 |
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 |
| C | TRP164-PRO189 | |
| A | TRP164-PRO189 |
| site_id | PS01164 |
| Number of Residues | 14 |
| Details | COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVVsqifTaaNYEY |
| Chain | Residue | Details |
| C | LEU394-TYR407 | |
| 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 |
| C | THR619-PRO632 | |
| A | THR619-PRO632 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:9551552 |
| Chain | Residue | Details |
| C | ASP319 | |
| D | ASP319 | |
| E | ASP319 | |
| F | ASP319 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| 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 |
| C | TPQ405 | |
| D | TPQ405 | |
| E | TPQ405 | |
| F | TPQ405 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5 |
| Chain | Residue | Details |
| C | ALA317 | |
| D | ALA317 | |
| E | ALA317 | |
| F | ALA317 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P46883 |
| Chain | Residue | Details |
| C | ALA402 | |
| D | ALA402 | |
| E | ALA402 | |
| F | ALA402 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| 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 |
| C | HIS456 | |
| F | HIS456 | |
| F | HIS458 | |
| F | HIS624 | |
| C | HIS458 | |
| C | HIS624 | |
| D | HIS456 | |
| D | HIS458 | |
| D | HIS624 | |
| E | HIS456 | |
| E | HIS458 | |
| E | HIS624 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q43077 |
| Chain | Residue | Details |
| C | ASP465 | |
| F | ASP465 | |
| F | ASP613 | |
| F | ILE614 | |
| C | ASP613 | |
| C | ILE614 | |
| D | ASP465 | |
| D | ASP613 | |
| D | ILE614 | |
| E | ASP465 | |
| E | ASP613 | |
| E | ILE614 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:2OQE |
| Chain | Residue | Details |
| C | TPQ405 | |
| D | TPQ405 | |
| E | TPQ405 | |
| F | TPQ405 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:9551552 |
| Chain | Residue | Details |
| C | ASN243 | |
| D | ASN243 | |
| E | ASN243 | |
| F | ASN243 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oac |
| Chain | Residue | Details |
| A | ASP319 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oac |
| Chain | Residue | Details |
| B | ASP319 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oac |
| Chain | Residue | Details |
| C | ASP319 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oac |
| Chain | Residue | Details |
| D | ASP319 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oac |
| Chain | Residue | Details |
| E | ASP319 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oac |
| Chain | Residue | Details |
| F | ASP319 |
