4A6E
Crystal structure of human N-acetylserotonin methyltransferase (ASMT) in complex with SAM and N-acetylserotonin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005829 | cellular_component | cytosol |
A | 0006412 | biological_process | translation |
A | 0006629 | biological_process | lipid metabolic process |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0008171 | molecular_function | O-methyltransferase activity |
A | 0008172 | molecular_function | S-methyltransferase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0017096 | molecular_function | acetylserotonin O-methyltransferase activity |
A | 0030187 | biological_process | melatonin biosynthetic process |
A | 0032259 | biological_process | methylation |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046219 | biological_process | indolalkylamine biosynthetic process |
A | 0046983 | molecular_function | protein dimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 1348 |
Chain | Residue |
A | GLU267 |
A | HIS271 |
A | HOH2033 |
A | HOH2047 |
A | HOH2048 |
site_id | AC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE SAM A 1349 |
Chain | Residue |
A | GLY187 |
A | ASP210 |
A | ILE211 |
A | VAL214 |
A | GLY235 |
A | ASP236 |
A | PHE237 |
A | PHE238 |
A | ALA251 |
A | ARG252 |
A | ASP256 |
A | ASE1350 |
A | HOH2013 |
A | HOH2018 |
A | HOH2019 |
A | HOH2049 |
A | PHE143 |
A | TYR147 |
A | LEU160 |
A | TRP164 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ASE A 1350 |
Chain | Residue |
A | MET105 |
A | TYR108 |
A | ARG252 |
A | HIS255 |
A | ASP256 |
A | TYR299 |
A | ASN302 |
A | GLN306 |
A | THR307 |
A | TYR338 |
A | SAM1349 |
A | HOH2027 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 1351 |
Chain | Residue |
A | LYS107 |
A | ARG111 |
A | GLN155 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1352 |
Chain | Residue |
A | GLU30 |
A | ARG111 |
A | ALA121 |
A | ARG125 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 1353 |
Chain | Residue |
A | LYS74 |
A | THR87 |
A | GLU88 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1354 |
Chain | Residue |
A | HIS318 |
A | ARG327 |
A | ASP328 |
A | PHE329 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 1355 |
Chain | Residue |
A | ARG115 |
A | PHE135 |
A | ARG148 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1356 |
Chain | Residue |
A | HIS264 |
A | ARG268 |
A | GLY346 |
A | THR347 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 1357 |
Chain | Residue |
A | LEU31 |
A | GLU39 |
A | GLY52 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:22775292 |
Chain | Residue | Details |
A | HIS255 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
A | TYR147 | |
A | TRP164 | |
A | ASP210 | |
A | GLY235 | |
A | ARG252 | |
A | ASP256 | |
A | ASN302 | |
A | GLN306 |