Structure of PDB 1uqu Chain A Binding Site BS01

Receptor Information
>1uqu Chain A (length=452) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SRLVVVSNRIAPPDSAGGLAVGILGALKAAGGLWFGWSGETGNEDQPLKK
VKKGNITWASFNLSEQDLDEYYNQFSNAVLWPAFHYRLDLVQFQRPAWDG
YLRVNALLADKLLPLLQDDDIIWIHDYHLLPFAHELRKRGVNNRIGFFLH
IPFPTPEIFNALPTYDTLLEQLCDYDLLGFQTENDRLAFLDCLSNLTRVT
TRSAKSHTAWGKAFRTEVYPIGIEPKEIAKQAAGPLPPKLAQLKAELKNV
QNIFSVERLDYSKGLPERFLAYEALLEKYPQHHGKIRYTQIAPTSRGDVQ
AYQDIRHQLENEAGRINGKYGQLGWTPLYYLNQHFDRKLLMKIFRYSDVG
LVTPLRDGMNLVAKEYVAAQDPANPGVLVLSQFAGAANELTSALIVNPYD
RDEVAAALDRALTMSLAERISRHAEMLDVIVKNDINHWQECFISDLKQIV
PR
Ligand information
Ligand IDUPG
InChIInChI=1S/C15H24N2O17P2/c18-3-5-8(20)10(22)12(24)14(32-5)33-36(28,29)34-35(26,27)30-4-6-9(21)11(23)13(31-6)17-2-1-7(19)16-15(17)25/h1-2,5-6,8-14,18,20-24H,3-4H2,(H,26,27)(H,28,29)(H,16,19,25)/t5-,6-,8-,9-,10+,11-,12-,13-,14-/m1/s1
InChIKeyHSCJRCZFDFQWRP-JZMIEXBBSA-N
SMILES
SoftwareSMILES
CACTVS 3.370OC[C@H]1O[C@H](O[P](O)(=O)O[P](O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N3C=CC(=O)NC3=O)[C@H](O)[C@@H](O)[C@@H]1O
ACDLabs 12.01O=C1C=CN(C(=O)N1)C2OC(C(O)C2O)COP(=O)(OP(=O)(OC3OC(C(O)C(O)C3O)CO)O)O
CACTVS 3.370OC[CH]1O[CH](O[P](O)(=O)O[P](O)(=O)OC[CH]2O[CH]([CH](O)[CH]2O)N3C=CC(=O)NC3=O)[CH](O)[CH](O)[CH]1O
OpenEye OEToolkits 1.7.6C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@](=O)(O)O[P@](=O)(O)O[C@@H]3[C@@H]([C@H]([C@@H]([C@H](O3)CO)O)O)O)O)O
OpenEye OEToolkits 1.7.6C1=CN(C(=O)NC1=O)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)OC3C(C(C(C(O3)CO)O)O)O)O)O
FormulaC15 H24 N2 O17 P2
NameURIDINE-5'-DIPHOSPHATE-GLUCOSE;
URIDINE-5'-MONOPHOSPHATE GLUCOPYRANOSYL-MONOPHOSPHATE ESTER
ChEMBLCHEMBL375951
DrugBankDB01861
ZINCZINC000008215472
PDB chain1uqu Chain A Residue 1457 [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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PDB1uqu The donor subsite of trehalose-6-phosphate synthase: binary complexes with UDP-glucose and UDP-2-deoxy-2-fluoro-glucose at 2 A resolution.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		H154 R262 K267 H338 F339 R341 L344 D361 G362 M363 N364 L365 V366 E369
Binding residue
(residue number reindexed from 1)		H150 R258 K263 H334 F335 R337 L340 D357 G358 M359 N360 L361 V362 E365
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) H154 D361
Catalytic site (residue number reindexed from 1) H150 D357
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:1uqu, PDBe:1uqu, PDBj:1uqu
PDBsum1uqu
PubMed14570926
UniProtP31677|OTSA_ECOLI Trehalose-6-phosphate synthase (Gene Name=otsA)

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