Structure of PDB 4pgh Chain B Binding Site BS01

Receptor Information
>4pgh Chain B (length=357) Species: 4558 (Sorghum bicolor) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EDVAAVADEEACMYAMQLASSSILPMTLKNALELGLLEVLQKDAGKALAA
EEVVARLPVAPTNPAAADMVDRMLRLLASYDVVKCQMEDKDGKYERRYSA
APVGKWLTPNEDGVSMAALALMNQDKVLMESWYYLKDAVLDGGIPFNKAY
GMTAFEYHGTDPRFNRVFNEGMKNHSVIITKKLLEFYTGFDESVSTLVDV
GGGIGATLHAITSHHSHIRGVNFDLPHVISEAPPFPGVQHVGGDMFKSVP
AGDAILMKWILHDWSDAHCATLLKNCYDALPEKGGKVIVVECVLPVTTDA
VPKAQGVFHVDMIMLAHNPGGRERYEREFRDLAKAAGFSGFKATYIYANA
WAIEFIK
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 chain4pgh Chain B Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4pgh Determination of the Structure and Catalytic Mechanism of Sorghum bicolor Caffeic Acid O-Methyltransferase and the Structural Impact of Three brown midrib12 Mutations.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		G206 D229 L230 D249 M250 F251 K263 I265
Binding residue
(residue number reindexed from 1)		G201 D224 L225 D244 M245 F246 K258 I260
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) H267 D268 E296 E328
Catalytic site (residue number reindexed from 1) H262 D263 E291 E323
Enzyme Commision number 2.1.1.68: caffeate O-methyltransferase.
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008171 O-methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0017096 acetylserotonin O-methyltransferase activity
GO:0030755 quercetin 3-O-methyltransferase activity
GO:0033799 myricetin 3'-O-methyltransferase activity
GO:0046983 protein dimerization activity
GO:0047763 caffeate O-methyltransferase activity
Biological Process
GO:0006970 response to osmotic stress
GO:0007623 circadian rhythm
GO:0009058 biosynthetic process
GO:0009809 lignin biosynthetic process
GO:0010344 seed oilbody biogenesis
GO:0010555 response to mannitol
GO:0030187 melatonin biosynthetic process
GO:0031537 regulation of anthocyanin metabolic process
GO:0032259 methylation
GO:0042428 serotonin metabolic process
GO:0048354 mucilage biosynthetic process involved in seed coat development
GO:0051555 flavonol biosynthetic process
GO:0090333 regulation of stomatal closure
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4pgh, PDBe:4pgh, PDBj:4pgh
PDBsum4pgh
PubMed24948836
UniProtC5YH12

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