Structure of PDB 2wtx Chain D Binding Site BS02

Receptor Information
>2wtx Chain D (length=457) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SRLVVVSNRIAPPDEHAASAGGLAVGILGALKAAGGLWFGWSGETGNEDQ
PLKKVKKGNITWASFNLSEQDLDEYYNQFSNAVLWPAFHYRLDLVQFQRP
AWDGYLRVNALLADKLLPLLQDDDIIWIHDYHLLPFAHELRKRGVNNRIG
FFLHIPFPTPEIFNALPTYDTLLEQLCDYDLLGFQTENDRLAFLDCLSNL
TRVTTRSAKSHTAWGKAFRTEVYPIGIEPKEIAKQAAGPLPPKLAQLKAE
LKNVQNIFSVERLDYSKGLPERFLAYEALLEKYPQHHGKIRYTQIAPTSR
GDVQAYQDIRHQLENEAGRINGKYGQLGWTPLYYLNQHFDRKLLMKIFRY
SDVGLVTPLRDGMNLVAKEYVAAQDPANPGVLVLSQFAGAANELTSALIV
NPYDRDEVAAALDRALTMSLAERISRHAEMLDVIVKNDINHWQECFISDL
KQIVPRS
Ligand information
Ligand IDVDO
InChIInChI=1S/C14H26NO11P/c16-3-5-1-7(11(19)13(21)9(5)17)15-8-2-6(4-26-27(23,24)25)10(18)14(22)12(8)20/h1,6-22H,2-4H2,(H2,23,24,25)/t6-,7+,8+,9-,10-,11+,12+,13+,14+/m1/s1
InChIKeyZKSTYMJGEHZSFH-MBABXGOBSA-N
SMILES
SoftwareSMILES
CACTVS 3.352OCC1=C[CH](N[CH]2C[CH](CO[P](O)(O)=O)[CH](O)[CH](O)[CH]2O)[CH](O)[CH](O)[CH]1O
OpenEye OEToolkits 1.6.1C1[C@@H]([C@H]([C@@H]([C@H]([C@H]1N[C@H]2C=C([C@H]([C@@H]([C@H]2O)O)O)CO)O)O)O)COP(=O)(O)O
OpenEye OEToolkits 1.6.1C1C(C(C(C(C1NC2C=C(C(C(C2O)O)O)CO)O)O)O)COP(=O)(O)O
CACTVS 3.352OCC1=C[C@H](N[C@H]2C[C@H](CO[P](O)(O)=O)[C@@H](O)[C@H](O)[C@H]2O)[C@H](O)[C@@H](O)[C@@H]1O
ACDLabs 10.04O=P(O)(O)OCC2C(O)C(O)C(O)C(NC1C=C(CO)C(O)C(O)C1O)C2
FormulaC14 H26 N O11 P
Name[(1R,2R,3S,4S,5S)-2,3,4-TRIHYDROXY-5-{[(1S,4R,5S,6S)-4,5,6-TRIHYDROXY-3-(HYDROXYMETHYL)CYCLOHEX-2-EN-1-YL]AMINO}CYCLOHEXYL]METHYL DIHYDROGEN PHOSPHATE
ChEMBL
DrugBank
ZINCZINC000058655549
PDB chain2wtx Chain D Residue 1459 [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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PDB2wtx Mechanistic Insight Into Enzymatic Glycosyl Transfer with Retention of Configuration Through Analysis of Glycomimetic Inhibitors.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		W85 D130 H154 R262 R300 D361 M363 N364
Binding residue
(residue number reindexed from 1)		W85 D130 H154 R262 R300 D361 M363 N364
Annotation score1
Binding affinityMOAD: Ki=1.3mM
Enzymatic activity
Catalytic site (original residue number in PDB) H154 D361
Catalytic site (residue number reindexed from 1) H154 D361
Enzyme Commision number 2.4.1.15: alpha,alpha-trehalose-phosphate synthase (UDP-forming).
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003825 alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity
GO:0016757 glycosyltransferase activity
GO:0016758 hexosyltransferase activity
Biological Process
GO:0005992 trehalose biosynthetic process
GO:0006950 response to stress
GO:0006970 response to osmotic stress
GO:0006974 DNA damage response
GO:0070415 trehalose metabolism in response to cold stress

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2wtx, PDBe:2wtx, PDBj:2wtx
PDBsum2wtx
PubMed20077550
UniProtP31677|OTSA_ECOLI Trehalose-6-phosphate synthase (Gene Name=otsA)

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