4EV2
Crystal structure of copper amine oxidase-1 from Hansenula polymorpha in complex with ethylamine
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 | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 701 |
| Chain | Residue |
| A | LYS561 |
| A | ASP593 |
| A | HOH822 |
| A | HOH1227 |
| C | TYR160 |
| C | LYS561 |
| C | SER591 |
| C | HOH1007 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 702 |
| Chain | Residue |
| A | HIS458 |
| A | HIS624 |
| A | PEO707 |
| A | HIS456 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 703 |
| Chain | Residue |
| A | HIS23 |
| A | TYR64 |
| A | LYS68 |
| A | VAL258 |
| A | LYS265 |
| A | ASP280 |
| A | HOH936 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 704 |
| Chain | Residue |
| A | HIS218 |
| A | LYS219 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 705 |
| Chain | Residue |
| A | GLU368 |
| A | LYS393 |
| A | ASP422 |
| A | ARG424 |
| A | HOH1117 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 706 |
| Chain | Residue |
| A | PRO484 |
| A | HOH1188 |
| A | HOH1275 |
| A | HOH1310 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEO A 707 |
| Chain | Residue |
| A | TYQ405 |
| A | LEU429 |
| A | HIS456 |
| A | HIS458 |
| A | HIS624 |
| A | MET634 |
| A | CU702 |
| A | HOH1365 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NEH A 708 |
| Chain | Residue |
| A | TRP156 |
| A | ALA317 |
| A | ASP319 |
| A | TYR323 |
| A | TYQ405 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 701 |
| Chain | Residue |
| B | LEU558 |
| B | LYS561 |
| B | SER591 |
| B | HOH827 |
| B | HOH1407 |
| F | LYS561 |
| F | ASP593 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 702 |
| Chain | Residue |
| B | HIS456 |
| B | HIS458 |
| B | HIS624 |
| B | PEO708 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 703 |
| Chain | Residue |
| B | GLU368 |
| B | LYS393 |
| B | ASP422 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 704 |
| Chain | Residue |
| B | HIS23 |
| B | TYR64 |
| B | LYS68 |
| B | LYS265 |
| B | ASP280 |
| B | HOH1059 |
| B | HOH1146 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL B 705 |
| Chain | Residue |
| A | PRO442 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 706 |
| Chain | Residue |
| B | ARG213 |
| B | LYS214 |
| B | VAL215 |
| B | ASP436 |
| B | HOH1305 |
| B | HOH1363 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 707 |
| Chain | Residue |
| A | TYR534 |
| B | HIS218 |
| B | LYS219 |
| B | TYR448 |
| B | PRO449 |
| B | HOH1450 |
| E | GLU69 |
| E | GLN70 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEO B 708 |
| Chain | Residue |
| B | TYQ405 |
| B | HIS456 |
| B | HIS458 |
| B | HIS624 |
| B | MET634 |
| B | CU702 |
| B | HOH839 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NEH B 709 |
| Chain | Residue |
| B | TRP156 |
| B | ALA317 |
| B | ASP319 |
| B | TYR323 |
| B | TYQ405 |
| B | HOH1308 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 710 |
| Chain | Residue |
| B | VAL250 |
| B | PHE252 |
| B | LYS253 |
| B | MET254 |
| B | HIS343 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU C 701 |
| Chain | Residue |
| C | HIS624 |
| C | HOH1225 |
| C | HOH1332 |
| C | HIS456 |
| C | HIS458 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 702 |
| Chain | Residue |
| C | HIS23 |
| C | TYR64 |
| C | LYS68 |
| C | LYS265 |
| C | ASP280 |
| C | HOH1279 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 703 |
| Chain | Residue |
| C | LYS393 |
| C | TYR410 |
| C | ARG420 |
| C | ASP422 |
| C | ARG424 |
| C | HOH1142 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 704 |
| Chain | Residue |
| C | ARG213 |
| C | LYS214 |
| C | VAL215 |
| C | ASP436 |
| C | HOH979 |
| C | HOH1072 |
| site_id | CC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 705 |
| Chain | Residue |
| C | GLU147 |
| C | TYR177 |
| C | SER216 |
| site_id | CC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL C 706 |
| Chain | Residue |
| C | PRO484 |
| D | TRP443 |
| site_id | CC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 707 |
| Chain | Residue |
| C | ASN514 |
| C | PRO550 |
| C | LEU551 |
| C | SER567 |
| C | HOH916 |
| site_id | CC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NEH C 708 |
| Chain | Residue |
| C | TRP156 |
| C | ALA317 |
| C | ASP319 |
| C | TYR323 |
| C | ALA402 |
| C | ALA403 |
| C | TYQ405 |
| site_id | CC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 C 709 |
| Chain | Residue |
| C | HIS218 |
| C | LYS219 |
| C | HOH1228 |
| site_id | DC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU D 701 |
| Chain | Residue |
| D | HIS456 |
| D | HIS458 |
| D | HIS624 |
| D | HOH1291 |
| site_id | DC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL D 702 |
| Chain | Residue |
| D | HIS23 |
| D | TYR64 |
| D | LYS68 |
| D | LYS265 |
| D | PHE266 |
| D | HIS267 |
| D | ASP280 |
| D | HOH1077 |
| site_id | DC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 703 |
| Chain | Residue |
| D | LEU512 |
| D | ASN514 |
| D | GLU516 |
| D | ARG521 |
| D | HOH1239 |
| site_id | DC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL D 704 |
| Chain | Residue |
| D | HOH1173 |
| site_id | DC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL D 705 |
| Chain | Residue |
| D | ILE342 |
| D | HIS343 |
| site_id | DC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NEH D 706 |
| Chain | Residue |
| D | ALA317 |
| D | ASP319 |
| D | TYR323 |
| D | ALA402 |
| D | TYQ405 |
| D | HOH1202 |
| site_id | DC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU E 701 |
| Chain | Residue |
| E | HIS456 |
| E | HIS458 |
| E | HIS624 |
| E | PEO706 |
| E | HOH1127 |
| site_id | DC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL E 702 |
| Chain | Residue |
| E | GLU368 |
| E | LYS393 |
| E | TYR410 |
| E | ASP422 |
| E | ARG424 |
| E | HOH932 |
| site_id | DC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL E 703 |
| Chain | Residue |
| E | HOH970 |
| E | HOH1031 |
| E | HOH1272 |
| site_id | EC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL E 704 |
| Chain | Residue |
| E | HIS23 |
| E | TYR64 |
| E | LYS68 |
| E | LYS265 |
| E | ASP280 |
| E | HOH929 |
| site_id | EC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL E 705 |
| Chain | Residue |
| E | GLU58 |
| E | PRO59 |
| E | TYR575 |
| E | ASN578 |
| E | LEU580 |
| E | HOH923 |
| E | HOH950 |
| E | HOH1020 |
| site_id | EC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEO E 706 |
| Chain | Residue |
| E | TYQ405 |
| E | HIS456 |
| E | MET634 |
| E | CU701 |
| E | HOH1045 |
| site_id | EC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NEH E 707 |
| Chain | Residue |
| E | ALA317 |
| E | ASP319 |
| E | TYR323 |
| E | TYQ405 |
| site_id | EC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU F 701 |
| Chain | Residue |
| F | HIS456 |
| F | HIS458 |
| F | HIS624 |
| F | PEO707 |
| site_id | EC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL F 702 |
| Chain | Residue |
| F | HIS23 |
| F | TYR64 |
| F | LYS68 |
| F | VAL258 |
| F | LYS265 |
| F | ASP280 |
| F | HOH1298 |
| site_id | EC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL F 703 |
| Chain | Residue |
| F | GLU58 |
| F | PRO59 |
| F | HIS294 |
| F | TYR575 |
| F | ASN578 |
| F | HOH890 |
| F | HOH924 |
| F | HOH988 |
| site_id | EC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL F 704 |
| Chain | Residue |
| E | GLY371 |
| F | LYS393 |
| F | ASP422 |
| F | ARG424 |
| F | HOH1256 |
| site_id | EC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL F 705 |
| Chain | Residue |
| F | ARG213 |
| F | LYS214 |
| F | VAL215 |
| F | ASP436 |
| F | ASN450 |
| F | HOH1220 |
| site_id | FC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL F 706 |
| Chain | Residue |
| E | PRO442 |
| F | TYR485 |
| F | HOH1101 |
| site_id | FC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEO F 707 |
| Chain | Residue |
| F | TYQ405 |
| F | HIS456 |
| F | HIS458 |
| F | HIS624 |
| F | MET634 |
| F | CU701 |
| F | HOH1125 |
| site_id | FC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NEH F 708 |
| Chain | Residue |
| F | TRP156 |
| F | ALA317 |
| F | ASP319 |
| F | TYR323 |
| F | ALA403 |
| F | TYQ405 |
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 | TYQ405 | |
| B | TYQ405 | |
| C | TYQ405 | |
| D | TYQ405 | |
| E | TYQ405 | |
| F | TYQ405 |
| 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 | TYQ405 | |
| B | TYQ405 | |
| C | TYQ405 | |
| D | TYQ405 | |
| E | TYQ405 | |
| F | TYQ405 |
| 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 |
