1D6Y
CRYSTAL STRUCTURE OF E. COLI COPPER-CONTAINING AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE AND COMPLEXED WITH NITRIC OXIDE.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005507 | molecular_function | copper ion binding |
A | 0005509 | molecular_function | calcium ion binding |
A | 0006559 | biological_process | L-phenylalanine catabolic process |
A | 0008131 | molecular_function | primary amine oxidase activity |
A | 0009308 | biological_process | amine metabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019607 | biological_process | phenylethylamine catabolic process |
A | 0042597 | cellular_component | periplasmic space |
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 | 0005509 | molecular_function | calcium ion binding |
B | 0006559 | biological_process | L-phenylalanine catabolic process |
B | 0008131 | molecular_function | primary amine oxidase activity |
B | 0009308 | biological_process | amine metabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019607 | biological_process | phenylethylamine catabolic process |
B | 0042597 | cellular_component | periplasmic space |
B | 0046872 | molecular_function | metal ion binding |
B | 0048038 | molecular_function | quinone binding |
B | 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 | HIS524 |
A | HIS526 |
A | HIS689 |
A | NO2002 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 802 |
Chain | Residue |
A | ALA679 |
A | HOH2140 |
A | LYS133 |
A | ASP533 |
A | LEU534 |
A | ASP535 |
A | ASP678 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 803 |
Chain | Residue |
A | GLU573 |
A | HIS644 |
A | TYR667 |
A | ASP670 |
A | GLU672 |
A | HOH2293 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU B 801 |
Chain | Residue |
B | HIS524 |
B | HIS526 |
B | HIS689 |
B | NO3002 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA B 802 |
Chain | Residue |
B | LYS133 |
B | ASP533 |
B | LEU534 |
B | ASP535 |
B | ASP678 |
B | ALA679 |
B | HOH3171 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 803 |
Chain | Residue |
B | GLU573 |
B | TYR667 |
B | GLU672 |
B | HOH3195 |
B | HOH3199 |
B | HOH3245 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE HY1 A 2001 |
Chain | Residue |
A | PHE192 |
A | THR223 |
A | LEU225 |
A | TRP257 |
A | TYR381 |
A | ASP383 |
A | TYR387 |
A | VAL463 |
A | GLY464 |
A | TYQ466 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NO A 2002 |
Chain | Residue |
A | TYQ466 |
A | HIS524 |
A | HIS526 |
A | HIS689 |
A | CU801 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEA A 2003 |
Chain | Residue |
A | ASP102 |
A | GLN106 |
A | LEU169 |
B | ALA56 |
B | GLN58 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE HY1 B 3001 |
Chain | Residue |
B | PHE192 |
B | LEU225 |
B | TRP257 |
B | TYR381 |
B | ASP383 |
B | TYR387 |
B | VAL463 |
B | GLY464 |
B | TYQ466 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NO B 3002 |
Chain | Residue |
B | TYQ466 |
B | GLU490 |
B | HIS524 |
B | HIS526 |
B | HIS689 |
B | CU801 |
B | HOH3043 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 2004 |
Chain | Residue |
A | ASN447 |
A | HOH2411 |
B | ARG425 |
B | HOH3029 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 3003 |
Chain | Residue |
B | ASP20 |
B | GLN307 |
B | SER404 |
Functional Information from PROSITE/UniProt
site_id | PS01164 |
Number of Residues | 14 |
Details | COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVVrwisTvgNYDY |
Chain | Residue | Details |
A | LEU455-TYR468 |
site_id | PS01165 |
Number of Residues | 14 |
Details | COPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TtGttHVaraEEwP |
Chain | Residue | Details |
A | THR684-PRO697 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:9048544, ECO:0007744|PDB:1OAC |
Chain | Residue | Details |
A | ASP383 | |
B | ASP383 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0000269|PubMed:10387067, ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAK, ECO:0007744|PDB:2WGQ, ECO:0007744|PDB:2WO0, ECO:0007744|PDB:2WOF |
Chain | Residue | Details |
A | TYQ466 | |
B | TYQ466 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10576737, ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y, ECO:0007744|PDB:1D6Z |
Chain | Residue | Details |
A | TYR381 | |
B | TYR381 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544, ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y, ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1LVN, ECO:0007744|PDB:1SPU |
Chain | Residue | Details |
A | VAL463 | |
B | VAL463 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544, ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y, ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU, ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN, ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF, ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL, ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q, ECO:0007744|PDB:2WGQ, ECO:0007744|PDB:2WO0, ECO:0007744|PDB:2WOF, ECO:0007744|PDB:2WOH |
Chain | Residue | Details |
A | HIS524 | |
A | HIS526 | |
A | HIS689 | |
B | HIS524 | |
B | HIS526 | |
B | HIS689 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q43077 |
Chain | Residue | Details |
A | ASP533 | |
A | ASP535 | |
A | ASP678 | |
B | ASP533 | |
B | ASP535 | |
B | ASP678 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544, ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y, ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU, ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN, ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF, ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL, ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q, ECO:0007744|PDB:2WGQ, ECO:0007744|PDB:2WOH |
Chain | Residue | Details |
A | LEU534 | |
B | LEU534 |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10387067, ECO:0000269|PubMed:10576737, ECO:0000269|PubMed:9048544, ECO:0007744|PDB:1D6U, ECO:0007744|PDB:1D6Y, ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU, ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1LVN, ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAF, ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL, ECO:0007744|PDB:1SPU, ECO:0007744|PDB:2W0Q, ECO:0007744|PDB:2WGQ |
Chain | Residue | Details |
A | GLU573 | |
A | TYR667 | |
A | GLU672 | |
B | GLU573 | |
B | TYR667 | |
B | GLU672 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10576737, ECO:0007744|PDB:1D6Y, ECO:0007744|PDB:1D6Z, ECO:0007744|PDB:1DYU, ECO:0007744|PDB:1OAC, ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL, ECO:0007744|PDB:2WGQ |
Chain | Residue | Details |
A | ASP670 | |
B | ASP670 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | ALA679 | |
B | ALA679 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:10387067, ECO:0007744|PDB:1DYU, ECO:0007744|PDB:1JRQ, ECO:0007744|PDB:1QAF, ECO:0007744|PDB:1QAK, ECO:0007744|PDB:1QAL |
Chain | Residue | Details |
A | TYQ466 | |
B | TYQ466 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oac |
Chain | Residue | Details |
A | ASP383 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oac |
Chain | Residue | Details |
B | ASP383 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 864 |
Chain | Residue | Details |
A | TYR369 | electrostatic stabiliser |
A | ASP383 | proton shuttle (general acid/base) |
A | TYQ466 | covalent catalysis |
A | HIS524 | metal ligand |
A | HIS526 | metal ligand |
A | HIS689 | metal ligand |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 864 |
Chain | Residue | Details |
B | TYR369 | electrostatic stabiliser |
B | ASP383 | proton shuttle (general acid/base) |
B | TYQ466 | covalent catalysis |
B | HIS524 | metal ligand |
B | HIS526 | metal ligand |
B | HIS689 | metal ligand |