Structure of PDB 1gz5 Chain D Binding Site BS01

Receptor Information
>1gz5 Chain D (length=455) Species: 316407 (Escherichia coli str. K-12 substr. W3110) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SRLVVVSNRIAPPDEHAASAGGLAVGILGALKAAGGLWFGWSGETGNEDQ
PLKKVKKGNITWASFNLSEQDLDEYYNQFSNAVLWPAFHYRLDLVQFQRP
AWDGYLRVNALLADKLLPLLQDDDIIWIHDYHLLPFAHELRKRGVNNRIG
FFLHIPFPTPEIFNALPTYDTLLEQLCDYDLLGFQTENDRLAFLDCLSNL
TRVTTRSKSHTAWGKAFRTEVYPIGIEPKEIAKQAAGPLPPKLAQLKAEL
KNVQNIFSVERLDYSKGLPERFLAYEALLEKYPQHHGKIRYTQIAPTSRG
DVQAYQDIRHQLENEAGRINGKYGQLGWTPLYYLNQHFDRKLLMKIFRYS
DVGLVTPLRDGMNLVAKEYVAAQDPANPGVLVLSQFAGAANELTSALIVN
PYDRDEVAAALDRALTMSLAERISRHAEMLDVIVKNDINHWQECFISDLK
QIVPR
Ligand information
Ligand IDUDP
InChIInChI=1S/C9H14N2O12P2/c12-5-1-2-11(9(15)10-5)8-7(14)6(13)4(22-8)3-21-25(19,20)23-24(16,17)18/h1-2,4,6-8,13-14H,3H2,(H,19,20)(H,10,12,15)(H2,16,17,18)/t4-,6-,7-,8-/m1/s1
InChIKeyXCCTYIAWTASOJW-XVFCMESISA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)(O)OP(=O)(O)O)O)O
CACTVS 3.370O[CH]1[CH](O)[CH](O[CH]1CO[P](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O
CACTVS 3.370O[C@H]1[C@@H](O)[C@@H](O[C@@H]1CO[P](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O
OpenEye OEToolkits 1.7.0C1=CN(C(=O)NC1=O)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)O)O)O
ACDLabs 12.01O=P(O)(O)OP(=O)(O)OCC2OC(N1C(=O)NC(=O)C=C1)C(O)C2O
FormulaC9 H14 N2 O12 P2
NameURIDINE-5'-DIPHOSPHATE
ChEMBLCHEMBL130266
DrugBankDB03435
ZINCZINC000004490939
PDB chain1gz5 Chain D Residue 900 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1gz5 Insights Into Trehalose Synthesis Provided by the Structure of the Retaining Glycosyltransferase Otsa
Resolution2.43 Å
Binding residue
(original residue number in PDB)		A20 G21 G22 V260 R262 K267 P297 F339 L344 L365 V366 E369
Binding residue
(residue number reindexed from 1)		A20 G21 G22 V259 R261 K266 P296 F338 L343 L364 V365 E368
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) H154 D361
Catalytic site (residue number reindexed from 1) H154 D360
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:1gz5, PDBe:1gz5, PDBj:1gz5
PDBsum1gz5
PubMed12498887
UniProtP31677|OTSA_ECOLI Trehalose-6-phosphate synthase (Gene Name=otsA)

[Back to BioLiP]