1KUX
X-ray Crystallographic Studies of Serotonin N-acetyltransferase Catalysis and Inhibition
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004059 | molecular_function | aralkylamine N-acetyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006474 | biological_process | N-terminal protein amino acid acetylation |
| A | 0007623 | biological_process | circadian rhythm |
| A | 0008080 | molecular_function | N-acetyltransferase activity |
| A | 0009416 | biological_process | response to light stimulus |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| A | 0030187 | biological_process | melatonin biosynthetic process |
| A | 0048471 | cellular_component | perinuclear region of cytoplasm |
| A | 0048511 | biological_process | rhythmic process |
| A | 0071320 | biological_process | cellular response to cAMP |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE CA3 A 900 |
| Chain | Residue |
| A | ALA55 |
| A | VAL126 |
| A | ARG131 |
| A | GLN132 |
| A | GLN133 |
| A | GLY134 |
| A | LYS135 |
| A | GLY136 |
| A | SER137 |
| A | ARG154 |
| A | MET159 |
| A | PHE56 |
| A | CYS160 |
| A | LEU164 |
| A | PHE167 |
| A | TYR168 |
| A | ARG170 |
| A | VAL183 |
| A | PHE188 |
| A | HOH504 |
| A | HOH508 |
| A | HOH513 |
| A | CYS63 |
| A | HOH517 |
| A | HOH527 |
| A | HOH561 |
| A | HOH592 |
| A | PRO64 |
| A | LEU121 |
| A | HIS122 |
| A | ALA123 |
| A | LEU124 |
| A | ALA125 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10319816","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11336675","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11902838","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11336675","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11884405","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11902838","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for the catalytic mechanism; involved in substrate deprotonation","evidences":[{"source":"PubMed","id":"10319816","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11884405","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by PKA","evidences":[{"source":"PubMed","id":"11427721","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14578935","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15644438","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1b6b |
| Chain | Residue | Details |
| A | SER97 | |
| A | LEU111 | |
| A | HIS122 | |
| A | LEU124 | |
| A | TYR168 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 22 |
| Chain | Residue | Details |
| A | SER97 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | LEU111 | hydrogen bond acceptor, steric role |
| A | HIS122 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | LEU124 | electrostatic stabiliser, hydrogen bond donor |
| A | TYR168 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
