2OQE
Crystal Structure of Hansenula polymorpha amine oxidase in complex with Xe to 1.6 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 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 |