Structure of PDB 4a6d Chain A Binding Site BS02

Receptor Information
>4a6d Chain A (length=345) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MGSSEDQAYRLLNDYANGFMVSQVLFAACELGVFDLLAEAPGPLDVAAVA
AGVRASAHGTELLLDICVSLKLLKVETRGGKAFYRNTELSSDYLTTVSPT
SQCSMLKYMGRTSYRCWGHLADAVREGRNQYLETFGVPAEELFTAIYRSE
GERLQFMQALQEVWSVNGRSVLTAFDLSVFPLMCDLGGGAGALAKECMSL
YPGCKITVFDIPEVVWTAKQHFSFEEQIDFQEGDFFKDPLPEADLYILAR
VLHDWADGKCSHLLERIYHTCKPGGGILVIESLLDEDRRGPLLTQLYSLN
MLVQTEGQERTPTHYHMLLSSAGFRDFQFKKTGAIYDAILARKGT
Ligand information
Ligand IDSAM
InChIInChI=1S/C15H22N6O5S/c1-27(3-2-7(16)15(24)25)4-8-10(22)11(23)14(26-8)21-6-20-9-12(17)18-5-19-13(9)21/h5-8,10-11,14,22-23H,2-4,16H2,1H3,(H2-,17,18,19,24,25)/t7-,8+,10+,11+,14+,27-/m0/s1
InChIKeyMEFKEPWMEQBLKI-FCKMPRQPSA-N
SMILES
SoftwareSMILES
CACTVS 3.341C[S@@+](CC[C@H](N)C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0C[S+](CCC(C(=O)[O-])N)CC1C(C(C(O1)n2cnc3c2ncnc3N)O)O
CACTVS 3.341C[S+](CC[CH](N)C([O-])=O)C[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0C[S@@+](CC[C@@H](C(=O)[O-])N)C[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)O
ACDLabs 10.04[O-]C(=O)C(N)CC[S+](C)CC3OC(n2cnc1c(ncnc12)N)C(O)C3O
FormulaC15 H22 N6 O5 S
NameS-ADENOSYLMETHIONINE
ChEMBLCHEMBL1235831
DrugBank
ZINC
PDB chain4a6d Chain A Residue 1350 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4a6d Crystal Structure and Functional Mapping of Human Asmt, the Last Enzyme of the Melatonin Synthesis Pathway.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		F143 Y147 L160 W164 G187 D210 I211 G235 D236 F237 A251 R252 D256
Binding residue
(residue number reindexed from 1)		F143 Y147 L160 W164 G187 D210 I211 G233 D234 F235 A249 R250 D254
Annotation score5
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.
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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Molecular Function
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Biological Process
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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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