Structure of PDB 1kuv Chain A

Receptor sequence
>1kuvA (length=166) Species: 9940 (Ovis aries) [Search protein sequence]
HTLPANEFRCLTPEDAAGVFEIEREAFISVSGNCPLNLDEVQHFLTLCPE
LSLGWFVEGRLVAFIIGSLWDEERLTQESLALHRPRGHSAHLHALAVHRS
FRQQGKGSVLLWRYLHHVGAQPAVRRAVLMCEDALVPFYQRFGFHPAGPC
AIVVGSLTFTEMHCSL
3D structure
PDB1kuv X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S97 L111 H122 L124 Y168
Catalytic site (residue number reindexed from 1) S68 L82 H93 L95 Y139
Enzyme Commision number 2.3.1.87: aralkylamine N-acetyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA5 A A55 F56 S60 C63 P64 A123 L124 A125 V126 R131 Q132 G134 G136 S137 M159 E161 L164 F167 Y168 R170 L186 F188 A26 F27 S31 C34 P35 A94 L95 A96 V97 R102 Q103 G105 G107 S108 M130 E132 L135 F138 Y139 R141 L157 F159 MOAD: Ki=22nM
Gene Ontology
Molecular Function
GO:0004059 aralkylamine N-acetyltransferase activity
GO:0005515 protein binding
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
Biological Process
GO:0006474 N-terminal protein amino acid acetylation
GO:0007623 circadian rhythm
GO:0009416 response to light stimulus
GO:0030187 melatonin biosynthetic process
GO:0048511 rhythmic process
GO:0071320 cellular response to cAMP
Cellular Component
GO:0005737 cytoplasm
GO:0048471 perinuclear region of cytoplasm

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Cellular Component
External links
PDB RCSB:1kuv, PDBe:1kuv, PDBj:1kuv
PDBsum1kuv
PubMed11902838
UniProtQ29495|SNAT_SHEEP Serotonin N-acetyltransferase (Gene Name=AANAT)

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