2Z5Y
Crystal Structure of Human Monoamine Oxidase A (G110A) with Harmine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005739 | cellular_component | mitochondrion |
A | 0005741 | cellular_component | mitochondrial outer membrane |
A | 0005829 | cellular_component | cytosol |
A | 0006576 | biological_process | biogenic amine metabolic process |
A | 0006584 | biological_process | catecholamine metabolic process |
A | 0008131 | molecular_function | primary amine oxidase activity |
A | 0009967 | biological_process | positive regulation of signal transduction |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0042420 | biological_process | dopamine catabolic process |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0052595 | molecular_function | aliphatic amine oxidase activity |
A | 0097621 | molecular_function | monoamine oxidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 37 |
Details | BINDING SITE FOR RESIDUE FAD A 600 |
Chain | Residue |
A | ILE19 |
A | ARG45 |
A | GLY49 |
A | GLY50 |
A | ARG51 |
A | GLY66 |
A | GLY67 |
A | ALA68 |
A | TYR69 |
A | PRO243 |
A | ALA272 |
A | GLY20 |
A | ILE273 |
A | LEU277 |
A | TRP397 |
A | TYR402 |
A | CYS406 |
A | TYR407 |
A | GLY434 |
A | THR435 |
A | GLY443 |
A | TYR444 |
A | GLY21 |
A | MET445 |
A | ALA448 |
A | HOH709 |
A | HOH723 |
A | HOH726 |
A | HOH731 |
A | HOH742 |
A | HOH745 |
A | GLY22 |
A | ILE23 |
A | SER24 |
A | LEU42 |
A | GLU43 |
A | ALA44 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE HRM A 700 |
Chain | Residue |
A | ILE180 |
A | ASN181 |
A | PHE208 |
A | GLN215 |
A | ILE335 |
A | LEU337 |
A | PHE352 |
A | TYR407 |
A | TYR444 |
A | HOH717 |
A | HOH882 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DCX A 1 |
Chain | Residue |
A | THR489 |
A | TRP491 |
A | GLU492 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DCX A 2 |
Chain | Residue |
A | TRP116 |
A | PRO118 |
A | TYR121 |
A | THR509 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Anchor for type IV membrane protein |
Chain | Residue | Details |
A | VAL498-LEU518 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Important for substrate specificity => ECO:0000250 |
Chain | Residue | Details |
A | ILE335 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | SITE: Important for catalytic activity |
Chain | Residue | Details |
A | CYS374 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P21396 |
Chain | Residue | Details |
A | SER383 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: S-8alpha-FAD cysteine => ECO:0000269|PubMed:18391214, ECO:0007744|PDB:2BXR, ECO:0007744|PDB:2BXS, ECO:0007744|PDB:2Z5X, ECO:0007744|PDB:2Z5Y |
Chain | Residue | Details |
A | CYS406 |