Structure of PDB 1guq Chain B Binding Site BS04

Receptor Information
>1guq Chain B (length=344) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TQFNPVDHPHRRYNPLTGQWILVSPHRAKRPWQGAQETPAKQVLPAHDPD
CFLCAGNVRVTGDKNPDYTGTYVFTNDFAALMSDTPDAPESHDPLMRCQS
ARGTSRVICFSPDHSKTLPELSVAALTEIVKTWQEQTAELGKTYPWVQVF
ENKGAAMGCSNPHPGGQIWANSFLPNEAEREDRLQKEYFAEQKSPMLVDY
VQRELADGSRTVVETEHWLAVVPYWAAWPFETLLLPKAHVLRITDLTDAQ
RSDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNGEENQHWQLHAHFYP
PLLRSATVRKFMVGYEMLAETQRDLTAEQAAERLRAVSDIHFRE
Ligand information
Ligand IDK
InChIInChI=1S/K/q+1
InChIKeyNPYPAHLBTDXSSS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[K+]
FormulaK
NamePOTASSIUM ION
ChEMBLCHEMBL1233793
DrugBankDB01345
ZINC
PDB chain1guq Chain B Residue 353 [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]
PDB1guq Structural analysis of the H166G site-directed mutant of galactose-1-phosphate uridylyltransferase complexed with either UDP-glucose or UDP-galactose: detailed description of the nucleotide sugar binding site.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		N153 K154 C160 G166 G167
Binding residue
(residue number reindexed from 1)		N152 K153 C159 G165 G166
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) C52 C55 H115 N153 S161 H164 G166 Q168
Catalytic site (residue number reindexed from 1) C51 C54 H114 N152 S160 H163 G165 Q167
Enzyme Commision number 2.7.7.12: UDP-glucose--hexose-1-phosphate uridylyltransferase.
Gene Ontology
Molecular Function
GO:0004335 galactokinase activity
GO:0008108 UDP-glucose:hexose-1-phosphate uridylyltransferase activity
GO:0008198 ferrous iron binding
GO:0008270 zinc ion binding
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006012 galactose metabolic process
GO:0033499 galactose catabolic process via UDP-galactose
GO:0046835 carbohydrate phosphorylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1guq, PDBe:1guq, PDBj:1guq
PDBsum1guq
PubMed9063869
UniProtP09148|GAL7_ECOLI Galactose-1-phosphate uridylyltransferase (Gene Name=galT)

[Back to BioLiP]