4EV5
Crystal structure of copper amine oxidase-1 from Hansenula polymorpha in complex with benzylamine
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 | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 701 |
Chain | Residue |
A | LYS561 |
A | ASP593 |
C | TYR160 |
C | LYS561 |
C | SER591 |
C | HOH1011 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU A 702 |
Chain | Residue |
A | PEO707 |
A | HIS456 |
A | HIS458 |
A | HIS624 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 703 |
Chain | Residue |
A | HIS23 |
A | TYR64 |
A | LYS68 |
A | LYS265 |
A | HIS267 |
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 | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 705 |
Chain | Residue |
A | GLU368 |
A | LYS393 |
A | ASP422 |
A | ARG424 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 706 |
Chain | Residue |
A | PRO484 |
A | TYR499 |
A | HOH1191 |
A | HOH1278 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PEO A 707 |
Chain | Residue |
A | TYQ405 |
A | LEU429 |
A | HIS456 |
A | HIS458 |
A | MET634 |
A | CU702 |
A | HOH1323 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ABN A 708 |
Chain | Residue |
A | TRP156 |
A | ALA317 |
A | ASP319 |
A | TYR323 |
A | ALA402 |
A | ALA403 |
A | TYQ405 |
A | HOH1324 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 701 |
Chain | Residue |
B | LEU558 |
B | LYS561 |
B | SER591 |
B | HOH1267 |
F | LYS561 |
F | ASP593 |
F | HOH819 |
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 | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 703 |
Chain | Residue |
B | GLU368 |
B | LYS393 |
B | TYR410 |
B | ASP422 |
B | ARG424 |
B | HOH1232 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 704 |
Chain | Residue |
B | HIS23 |
B | TYR64 |
B | LYS68 |
B | LYS265 |
B | ASP280 |
B | HOH1054 |
site_id | BC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE GOL B 705 |
Chain | Residue |
B | TYR499 |
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 | HOH1292 |
B | HOH1351 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 707 |
Chain | Residue |
A | TYR534 |
B | HIS218 |
B | LYS219 |
B | TYR448 |
B | HOH1376 |
E | GLU69 |
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 | HOH837 |
site_id | BC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ABN B 709 |
Chain | Residue |
B | LEU121 |
B | TRP156 |
B | ALA317 |
B | ASP319 |
B | TYR323 |
B | ALA402 |
B | ALA403 |
B | TYQ405 |
B | HOH1295 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU C 701 |
Chain | Residue |
C | HIS456 |
C | HIS458 |
C | HIS624 |
C | HOH1235 |
C | HOH1295 |
site_id | CC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 702 |
Chain | Residue |
C | HIS23 |
C | TYR64 |
C | VAL258 |
C | LYS265 |
C | HIS267 |
C | ASP280 |
C | HOH1288 |
site_id | CC2 |
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 | HOH1152 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL C 704 |
Chain | Residue |
C | LYS214 |
C | VAL215 |
C | ASP436 |
C | HOH982 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL C 705 |
Chain | Residue |
C | PRO144 |
C | TYR177 |
C | SER216 |
site_id | CC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL C 706 |
Chain | Residue |
C | TYR499 |
D | TRP443 |
site_id | CC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 707 |
Chain | Residue |
C | PRO550 |
C | LEU551 |
C | SER567 |
C | HOH919 |
D | HOH1087 |
site_id | CC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ABN C 708 |
Chain | Residue |
C | LEU121 |
C | TRP156 |
C | ALA317 |
C | ASP319 |
C | TYR323 |
C | ALA402 |
C | ALA403 |
C | TYQ405 |
site_id | CC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU D 701 |
Chain | Residue |
D | HIS456 |
D | HIS458 |
D | HIS624 |
D | HOH1257 |
site_id | CC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL D 702 |
Chain | Residue |
D | HIS23 |
D | TYR64 |
D | LYS68 |
D | LYS265 |
D | HIS267 |
D | ASP280 |
site_id | DC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL D 703 |
Chain | Residue |
D | LEU512 |
D | ASN514 |
D | GLU516 |
D | ARG521 |
D | HOH1237 |
site_id | DC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL D 704 |
Chain | Residue |
D | TYR499 |
D | HOH1167 |
site_id | DC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL D 705 |
Chain | Residue |
D | ILE342 |
D | HIS343 |
site_id | DC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ABN D 706 |
Chain | Residue |
D | PRO155 |
D | TRP156 |
D | ALA317 |
D | ASP319 |
D | TYR323 |
D | ALA402 |
D | ALA403 |
D | TYQ405 |
D | HOH1199 |
site_id | DC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU E 701 |
Chain | Residue |
E | HIS456 |
E | HIS458 |
E | HIS624 |
E | PEO705 |
site_id | DC6 |
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 | HOH934 |
site_id | DC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL E 703 |
Chain | Residue |
E | TYR499 |
E | HOH974 |
E | HOH1037 |
site_id | DC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL E 704 |
Chain | Residue |
E | HIS23 |
E | TYR64 |
E | LYS68 |
E | LYS265 |
E | PHE266 |
E | ASP280 |
E | HOH931 |
site_id | DC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PEO E 705 |
Chain | Residue |
E | TYQ405 |
E | HIS456 |
E | HIS458 |
E | MET634 |
E | CU701 |
E | HOH1048 |
site_id | EC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL E 706 |
Chain | Residue |
E | GLU58 |
E | PRO59 |
E | ARG463 |
E | TYR575 |
E | ASN578 |
E | HOH925 |
E | HOH954 |
site_id | EC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ABN E 707 |
Chain | Residue |
E | TRP156 |
E | ALA317 |
E | ASP319 |
E | TYR323 |
E | ALA402 |
E | ALA403 |
E | TYQ405 |
E | HOH1258 |
site_id | EC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU F 701 |
Chain | Residue |
F | HIS456 |
F | HIS458 |
F | HIS624 |
F | PEO707 |
site_id | EC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL F 702 |
Chain | Residue |
F | HIS23 |
F | TYR64 |
F | LYS68 |
F | VAL258 |
F | LYS265 |
F | ASP280 |
site_id | EC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL F 703 |
Chain | Residue |
F | GLU58 |
F | HIS294 |
F | ARG463 |
F | TYR575 |
F | ASN578 |
F | HOH921 |
F | HOH982 |
F | HOH1045 |
site_id | EC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL F 704 |
Chain | Residue |
E | GLY371 |
F | GLU368 |
F | LYS393 |
F | TYR410 |
F | ASP422 |
F | ARG424 |
F | HOH1256 |
site_id | EC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL F 705 |
Chain | Residue |
F | ARG213 |
F | LYS214 |
F | VAL215 |
F | ASP436 |
F | ASN450 |
F | HOH1218 |
F | HOH1299 |
site_id | EC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL F 706 |
Chain | Residue |
F | PRO484 |
F | HOH1096 |
site_id | EC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PEO F 707 |
Chain | Residue |
F | TYQ405 |
F | HIS456 |
F | HIS458 |
F | MET634 |
F | CU701 |
F | HOH1122 |
site_id | FC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ABN F 708 |
Chain | Residue |
F | LEU121 |
F | TRP156 |
F | ALA317 |
F | ASP319 |
F | TYR323 |
F | ALA402 |
F | ALA403 |
F | TYQ405 |
F | HOH1003 |
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 |