2C72
Functional Role of the Aromatic Cage in Human Monoamine Oxidase B: Structures and Catalytic Properties of Tyr435 Mutant Proteins
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005739 | cellular_component | mitochondrion |
A | 0005740 | cellular_component | mitochondrial envelope |
A | 0005741 | cellular_component | mitochondrial outer membrane |
A | 0008131 | molecular_function | primary methylamine oxidase activity |
A | 0009055 | molecular_function | electron transfer activity |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0021762 | biological_process | substantia nigra development |
A | 0042420 | biological_process | dopamine catabolic process |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0050665 | biological_process | hydrogen peroxide biosynthetic process |
A | 0097621 | molecular_function | monoamine oxidase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005739 | cellular_component | mitochondrion |
B | 0005740 | cellular_component | mitochondrial envelope |
B | 0005741 | cellular_component | mitochondrial outer membrane |
B | 0008131 | molecular_function | primary methylamine oxidase activity |
B | 0009055 | molecular_function | electron transfer activity |
B | 0016020 | cellular_component | membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0021762 | biological_process | substantia nigra development |
B | 0042420 | biological_process | dopamine catabolic process |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0050665 | biological_process | hydrogen peroxide biosynthetic process |
B | 0097621 | molecular_function | monoamine oxidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 39 |
Details | BINDING SITE FOR RESIDUE FAD A 600 |
Chain | Residue |
A | VAL10 |
A | GLY40 |
A | GLY41 |
A | ARG42 |
A | THR43 |
A | GLY58 |
A | SER59 |
A | TYR60 |
A | PRO234 |
A | VAL235 |
A | ALA263 |
A | GLY11 |
A | ILE264 |
A | TRP388 |
A | TYR393 |
A | CYS397 |
A | TYR398 |
A | GLY425 |
A | THR426 |
A | GLY434 |
A | HIS435 |
A | MET436 |
A | GLY13 |
A | ALA439 |
A | RSA601 |
A | HOH2007 |
A | HOH2092 |
A | HOH2155 |
A | HOH2156 |
A | HOH2157 |
A | HOH2158 |
A | HOH2159 |
A | HOH2160 |
A | ILE14 |
A | SER15 |
A | LEU33 |
A | GLU34 |
A | ALA35 |
A | ARG36 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE RSA A 601 |
Chain | Residue |
A | LEU171 |
A | CYS172 |
A | ILE198 |
A | ILE199 |
A | GLN206 |
A | TYR326 |
A | TYR398 |
A | FAD600 |
site_id | AC3 |
Number of Residues | 39 |
Details | BINDING SITE FOR RESIDUE FAD B 600 |
Chain | Residue |
B | VAL10 |
B | GLY11 |
B | GLY13 |
B | ILE14 |
B | SER15 |
B | LEU33 |
B | GLU34 |
B | ALA35 |
B | ARG36 |
B | GLY40 |
B | GLY41 |
B | ARG42 |
B | THR43 |
B | GLY58 |
B | SER59 |
B | TYR60 |
B | PRO234 |
B | VAL235 |
B | ALA263 |
B | ILE264 |
B | TRP388 |
B | TYR393 |
B | CYS397 |
B | TYR398 |
B | GLY425 |
B | THR426 |
B | GLY434 |
B | HIS435 |
B | MET436 |
B | ALA439 |
B | RSA601 |
B | HOH2027 |
B | HOH2157 |
B | HOH2189 |
B | HOH2190 |
B | HOH2191 |
B | HOH2192 |
B | HOH2193 |
B | HOH2194 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE RSA B 601 |
Chain | Residue |
B | LEU171 |
B | CYS172 |
B | ILE198 |
B | ILE199 |
B | GLN206 |
B | TYR326 |
B | TYR398 |
B | FAD600 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 974 |
Details | TOPO_DOM: Cytoplasmic |
Chain | Residue | Details |
A | ASN3-PRO490 | |
B | ASN3-PRO490 |
site_id | SWS_FT_FI2 |
Number of Residues | 52 |
Details | TRANSMEM: Helical; Anchor for type IV membrane protein |
Chain | Residue | Details |
A | GLY491-LEU517 | |
B | GLY491-LEU517 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | TOPO_DOM: Mitochondrial intermembrane |
Chain | Residue | Details |
A | LEU517-VAL520 | |
B | LEU517-VAL520 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | SITE: Important for catalytic activity |
Chain | Residue | Details |
A | TRP157 | |
A | GLU366 | |
A | TYR383 | |
B | TRP157 | |
B | GLU366 | |
B | TYR383 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:11049757 |
Chain | Residue | Details |
A | ASN3 | |
B | ASN3 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8BW75 |
Chain | Residue | Details |
A | TYR53 | |
B | TYR53 |
Chain | Residue | Details |
A | TYR398 | |
B | TYR398 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1b5q |
Chain | Residue | Details |
A | GLY62 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1b5q |
Chain | Residue | Details |
B | GLY62 |