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1L0C

Investigation of the Roles of Catalytic Residues in Serotonin N-Acetyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004059molecular_functionaralkylamine N-acetyltransferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006474biological_processN-terminal protein amino acid acetylation
A0007623biological_processcircadian rhythm
A0009416biological_processresponse to light stimulus
A0016410molecular_functionN-acyltransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0030187biological_processmelatonin biosynthetic process
A0048471cellular_componentperinuclear region of cytoplasm
A0048511biological_processrhythmic process
A0071320biological_processcellular response to cAMP
Functional Information from PDB Data
site_idAC1
Number of Residues30
DetailsBINDING SITE FOR RESIDUE COT A 900
ChainResidue
AALA55
AALA125
AVAL126
AARG131
AGLN132
AGLN133
AGLY134
AGLY136
ASER137
AARG154
AMET159
APHE56
ACYS160
AALA163
ALEU164
APHE167
APHE168
AARG170
AVAL183
AHOH927
AHOH940
AHOH970
ASER60
AHOH978
AASN62
ACYS63
APRO64
AHIS122
AALA123
ALEU124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11336675, ECO:0000269|PubMed:11884405, ECO:0000269|PubMed:11902838
ChainResidueDetails
ALEU124
AMET159

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10319816, ECO:0000269|PubMed:11336675, ECO:0000269|PubMed:11902838
ChainResidueDetails
APHE168
AGLN132

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Important for the catalytic mechanism; involved in substrate deprotonation => ECO:0000269|PubMed:10319816, ECO:0000269|PubMed:11884405
ChainResidueDetails
AHIS120
AHIS122

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKA => ECO:0000269|PubMed:11427721, ECO:0000269|PubMed:14578935, ECO:0000269|PubMed:15644438
ChainResidueDetails
ATHR31

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:15644438
ChainResidueDetails
ASER205

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 22
ChainResidueDetails
ASER97activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
ALEU111hydrogen bond acceptor, steric role
AHIS122hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ALEU124electrostatic stabiliser, hydrogen bond donor
APHE168electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-06-12

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