Structure of PDB 2cl5 Chain B Binding Site BS03

Receptor Information
>2cl5 Chain B (length=214) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MGDTKEQRILRYVQQNAKPGDPQSVLEAIDTYCTQKEWAMNVGDAKGQIM
DAVIREYSPSLVLELGAYCGYSAVRMARLLQPGARLLTMEMNPDYAAITQ
QMLNFAGLQDKVTILNGASQDLIPQLKKKYDVDTLDMVFLDHWKDRYLPD
TLLLEKCGLLRKGTVLLADNVIVPGTPDFLAYVRGSSSFECTHYSSYLEY
MKVVDGLEKAIYQG
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 chain2cl5 Chain B Residue 1217 [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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PDB2cl5 Comparative Study of Ortho- and Meta-Nitrated Inhibitors of Catechol-O-Methyltransferase: Interactions with the Active Site and Regioselectivity of O-Methylation.
Resolution1.6 Å
Binding residue
(original residue number in PDB)		M40 N41 V42 G66 Y68 Y71 S72 E90 M91 Y95 A118 S119 D141 H142 W143
Binding residue
(residue number reindexed from 1)		M40 N41 V42 G66 Y68 Y71 S72 E90 M91 Y95 A118 S119 D141 H142 W143
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) D141 K144 D169 N170 E199
Catalytic site (residue number reindexed from 1) D141 K144 D169 N170 E199
Enzyme Commision number 2.1.1.6: catechol O-methyltransferase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008171 O-methyltransferase activity
GO:0016206 catechol O-methyltransferase activity
Biological Process
GO:0006584 catecholamine metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2cl5, PDBe:2cl5, PDBj:2cl5
PDBsum2cl5
PubMed16618795
UniProtP22734|COMT_RAT Catechol O-methyltransferase (Gene Name=Comt)

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