3NBJ
Crystal Structure of Y305F mutant of the copper amine oxidase from Hansenula polymorpha expressed in yeast
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 701 |
Chain | Residue |
A | TY8405 |
A | HIS456 |
A | HIS458 |
A | HIS624 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 702 |
Chain | Residue |
A | PRO209 |
A | ASN210 |
A | ARG211 |
A | HOH1250 |
A | HOH1373 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PO4 A 703 |
Chain | Residue |
A | HIS218 |
A | LYS219 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 704 |
Chain | Residue |
A | GLY594 |
A | VAL595 |
A | ARG596 |
A | HOH1324 |
A | HOH1393 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU B 701 |
Chain | Residue |
B | TY8405 |
B | HIS456 |
B | HIS458 |
B | HIS624 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B 702 |
Chain | Residue |
B | PRO209 |
B | ASN210 |
B | ARG211 |
B | HOH1250 |
B | HOH1373 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PO4 B 703 |
Chain | Residue |
B | HIS218 |
B | LYS219 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B 704 |
Chain | Residue |
B | GLY594 |
B | VAL595 |
B | ARG596 |
B | HOH1324 |
B | HOH1393 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU C 701 |
Chain | Residue |
C | TY8405 |
C | HIS456 |
C | HIS458 |
C | HIS624 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 C 702 |
Chain | Residue |
C | PRO209 |
C | ASN210 |
C | ARG211 |
C | HOH1250 |
C | HOH1373 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PO4 C 703 |
Chain | Residue |
C | HIS218 |
C | LYS219 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 C 704 |
Chain | Residue |
C | GLY594 |
C | VAL595 |
C | ARG596 |
C | HOH1324 |
C | HOH1393 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU D 701 |
Chain | Residue |
D | TY8405 |
D | HIS456 |
D | HIS458 |
D | HIS624 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 D 702 |
Chain | Residue |
D | PRO209 |
D | ASN210 |
D | ARG211 |
D | HOH1250 |
D | HOH1373 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PO4 D 703 |
Chain | Residue |
D | HIS218 |
D | LYS219 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 D 704 |
Chain | Residue |
D | GLY594 |
D | VAL595 |
D | ARG596 |
D | HOH1324 |
D | HOH1393 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU E 701 |
Chain | Residue |
E | TY8405 |
E | HIS456 |
E | HIS458 |
E | HIS624 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 E 702 |
Chain | Residue |
E | PRO209 |
E | ASN210 |
E | ARG211 |
E | HOH1250 |
E | HOH1373 |
site_id | CC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PO4 E 703 |
Chain | Residue |
E | HIS218 |
E | LYS219 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 E 704 |
Chain | Residue |
E | GLY594 |
E | VAL595 |
E | ARG596 |
E | HOH1324 |
E | HOH1393 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU F 701 |
Chain | Residue |
F | TY8405 |
F | HIS456 |
F | HIS458 |
F | HIS624 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 F 702 |
Chain | Residue |
F | PRO209 |
F | ASN210 |
F | ARG211 |
F | HOH1250 |
F | HOH1373 |
site_id | CC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PO4 F 703 |
Chain | Residue |
F | HIS218 |
F | LYS219 |
site_id | CC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 F 704 |
Chain | Residue |
F | GLY594 |
F | VAL595 |
F | ARG596 |
F | HOH1324 |
F | HOH1393 |
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 | 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 | TY8405 | |
B | TY8405 | |
C | TY8405 | |
D | TY8405 | |
E | TY8405 | |
F | TY8405 |
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 | TY8405 | |
B | TY8405 | |
C | TY8405 | |
D | TY8405 | |
E | TY8405 | |
F | TY8405 |
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 |