Structure of PDB 4a6d Chain A

Receptor sequence
>4a6dA (length=345) Species: 9606 (Homo sapiens) [Search protein sequence]
MGSSEDQAYRLLNDYANGFMVSQVLFAACELGVFDLLAEAPGPLDVAAVA
AGVRASAHGTELLLDICVSLKLLKVETRGGKAFYRNTELSSDYLTTVSPT
SQCSMLKYMGRTSYRCWGHLADAVREGRNQYLETFGVPAEELFTAIYRSE
GERLQFMQALQEVWSVNGRSVLTAFDLSVFPLMCDLGGGAGALAKECMSL
YPGCKITVFDIPEVVWTAKQHFSFEEQIDFQEGDFFKDPLPEADLYILAR
VLHDWADGKCSHLLERIYHTCKPGGGILVIESLLDEDRRGPLLTQLYSLN
MLVQTEGQERTPTHYHMLLSSAGFRDFQFKKTGAIYDAILARKGT
3D structure
PDB4a6d Crystal Structure and Functional Mapping of Human Asmt, the Last Enzyme of the Melatonin Synthesis Pathway.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H255 D256 E283 E311
Catalytic site (residue number reindexed from 1) H253 D254 E281 E309
Enzyme Commision number 2.1.1.4: acetylserotonin O-methyltransferase.
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 ZN A E267 H271 E265 H269
BS02 SAM A F143 Y147 L160 W164 G187 D210 I211 G235 D236 F237 A251 R252 D256 F143 Y147 L160 W164 G187 D210 I211 G233 D234 F235 A249 R250 D254
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008171 O-methyltransferase activity
GO:0008172 S-methyltransferase activity
GO:0017096 acetylserotonin O-methyltransferase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006412 translation
GO:0006629 lipid metabolic process
GO:0030187 melatonin biosynthetic process
GO:0032259 methylation
GO:0046219 indolalkylamine biosynthetic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:4a6d, PDBe:4a6d, PDBj:4a6d
PDBsum4a6d
PubMed22775292
UniProtP46597|ASMT_HUMAN Acetylserotonin O-methyltransferase (Gene Name=ASMT)

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