1D6Z
CRYSTAL STRUCTURE OF THE AEROBICALLY FREEZE TRAPPED RATE-DETERMINING CATALYTIC INTERMEDIATE OF E. COLI COPPER-CONTAINING AMINE OXIDASE.
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 methylamine 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 methylamine 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 | PEO2002 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 802 |
| Chain | Residue |
| A | ALA679 |
| A | HOH2141 |
| 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 | HOH2292 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 801 |
| Chain | Residue |
| B | HIS524 |
| B | HIS526 |
| B | HIS689 |
| B | PEO3002 |
| 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 | HOH3175 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 803 |
| Chain | Residue |
| B | GLU573 |
| B | TYR667 |
| B | GLU672 |
| B | HOH3199 |
| B | HOH3203 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE HY1 A 2001 |
| Chain | Residue |
| A | PRO224 |
| A | LEU225 |
| A | TRP257 |
| A | TYR381 |
| A | ASP383 |
| A | TYR387 |
| A | VAL463 |
| A | GLY464 |
| A | TYY466 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEO A 2002 |
| Chain | Residue |
| A | TYY466 |
| A | GLU490 |
| A | HIS524 |
| A | HIS526 |
| A | CU801 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEA A 2003 |
| Chain | Residue |
| A | GLN106 |
| A | LEU169 |
| A | HOH2747 |
| B | ALA56 |
| B | LEU57 |
| B | GLN58 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE HY1 B 3001 |
| Chain | Residue |
| B | LEU225 |
| B | TRP257 |
| B | TYR381 |
| B | ASP383 |
| B | TYR387 |
| B | VAL463 |
| B | GLY464 |
| B | TYY466 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEO B 3002 |
| Chain | Residue |
| B | TYY466 |
| B | GLU490 |
| B | HIS524 |
| B | HIS526 |
| B | CU801 |
| B | HOH3047 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 2004 |
| Chain | Residue |
| A | ARG452 |
| A | HIS475 |
| A | ASN477 |
| A | THR479 |
| A | LYS709 |
| B | THR612 |
| B | ARG692 |
| B | GLU702 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 3003 |
| Chain | Residue |
| B | ASP20 |
| 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 | TYY466 | |
| B | TYY466 |
| 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 | TYY466 | |
| B | TYY466 |
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 | TYY466 | 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 | TYY466 | covalent catalysis |
| B | HIS524 | metal ligand |
| B | HIS526 | metal ligand |
| B | HIS689 | metal ligand |
