Structure of PDB 5l6v Chain J Binding Site BS02

Receptor Information
>5l6v Chain J (length=412) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HLMLARQLPLKSVALILAGGRGTRLKDLTNKRAKPAVHFGGKFRIIDFAL
SNCINSGIRRMGVITQYQSHTLVQHIQRGWSFFNEEMNEFVDLLPARGTA
DAVTQNLDIIRRYKAEYVVILAGDHIYKQDYSRMLIDHVEKGARCTVACM
PVPIEEASAFGVMAVDENDKIIEFVEKPANPPSMPNDPSKSLASMGIYVF
DADYLYELLEEDDRDENSSHDFGKDLIPKITEAGLAYAHPFPLSCVQSDP
DAEPYWRDVGTLEAYWKANLDLASVVPELDMYDRNWPIRTYNESLPPAKF
VQDRSGSHGMTLNSLVSGGCVISGSVVVQSVLFSRVRVNSFCNIDSAVLL
PEVWVGRSCRLRRCVIDRACVIPEGMVIGENAEEDARRFYRSEEGIVLVT
REMLRKLGHKQE
Ligand information
Ligand IDFRU
InChIInChI=1S/C6H12O6/c7-1-3-4(9)5(10)6(11,2-8)12-3/h3-5,7-11H,1-2H2/t3-,4-,5+,6-/m1/s1
InChIKeyRFSUNEUAIZKAJO-ARQDHWQXSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04OC1C(O)C(OC1(O)CO)CO
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@@H]([C@](O1)(CO)O)O)O)O
CACTVS 3.341OC[CH]1O[C](O)(CO)[CH](O)[CH]1O
OpenEye OEToolkits 1.5.0C(C1C(C(C(O1)(CO)O)O)O)O
CACTVS 3.341OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O
FormulaC6 H12 O6
Namebeta-D-fructofuranose;
beta-D-fructose;
D-fructose;
fructose
ChEMBLCHEMBL604608
DrugBank
ZINCZINC000001529270
PDB chain5l6v Chain V Residue 2 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5l6v Structural Basis of Glycogen Biosynthesis Regulation in Bacteria.
Resolution2.667 Å
Binding residue
(original residue number in PDB)		D142 H143 K195
Binding residue
(residue number reindexed from 1)		D124 H125 K177
Annotation score1
Enzymatic activity
Enzyme Commision number 2.7.7.27: glucose-1-phosphate adenylyltransferase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0005524 ATP binding
GO:0008878 glucose-1-phosphate adenylyltransferase activity
GO:0016208 AMP binding
GO:0016779 nucleotidyltransferase activity
GO:0042802 identical protein binding
Biological Process
GO:0005978 glycogen biosynthetic process
GO:0009058 biosynthetic process
GO:0051289 protein homotetramerization
Cellular Component
GO:0010170 glucose-1-phosphate adenylyltransferase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5l6v, PDBe:5l6v, PDBj:5l6v
PDBsum5l6v
PubMed27545622
UniProtP0A6V1|GLGC_ECOLI Glucose-1-phosphate adenylyltransferase (Gene Name=glgC)

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