Structure of PDB 4pgh Chain A Binding Site BS01

Receptor Information
>4pgh Chain A (length=354) Species: 4558 (Sorghum bicolor) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AAVADEEACMYAMQLASSSILPMTLKNALELGLLEVLQKDAGKALAAEEV
VARLPVAPTNPAAADMVDRMLRLLASYDVVKCQMEDKDGKYERRYSAAPV
GKWLTPNEDGVSMAALALMNQDKVLMESWYYLKDAVLDGGIPFNKAYGMT
AFEYHGTDPRFNRVFNEGMKNHSVIITKKLLEFYTGFDESVSTLVDVGGG
IGATLHAITSHHSHIRGVNFDLPHVISEAPPFPGVQHVGGDMFKSVPAGD
AILMKWILHDWSDAHCATLLKNCYDALPEKGGKVIVVECVLPVTTDAVPK
AQGVFHVDMIMLAHNPGGRERYEREFRDLAKAAGFSGFKATYIYANAWAI
EFIK
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 A Residue 401 [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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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 K263
Binding residue
(residue number reindexed from 1)		G198 D221 L222 D241 M242 K255
Annotation score5
Binding affinityPDBbind-CN: -logKd/Ki=4.89,Kd=13uM
Enzymatic activity
Catalytic site (original residue number in PDB) H267 D268 E296 E328
Catalytic site (residue number reindexed from 1) H259 D260 E288 E320
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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