Structure of PDB 3upk Chain A Binding Site BS01

Receptor Information
>3upk Chain A (length=419) Species: 550 (Enterobacter cloacae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDI
DTTMKLLTQLGTKVERDGSVWIDASNVNNFSAPYDLVKTMRASIWALGPL
VARFGQGQVSLPGGCAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNGR
LKGAHIVMDKVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVA
LGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLVAAAISGGKIV
CRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGKRPKAVTVRTAPHP
AFPTDMQAQFTLLNLVAEGTGVITETIFENRFMHVPELIRMGAHAEIESN
TVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYE
RIEDKLRALGANIERVKGE
Ligand information
Ligand IDUD1
InChIInChI=1S/C17H27N3O17P2/c1-6(22)18-10-13(26)11(24)7(4-21)35-16(10)36-39(31,32)37-38(29,30)33-5-8-12(25)14(27)15(34-8)20-3-2-9(23)19-17(20)28/h2-3,7-8,10-16,21,24-27H,4-5H2,1H3,(H,18,22)(H,29,30)(H,31,32)(H,19,23,28)/t7-,8-,10-,11-,12-,13-,14-,15-,16-/m1/s1
InChIKeyLFTYTUAZOPRMMI-CFRASDGPSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(=O)NC1C(C(C(OC1OP(=O)(O)OP(=O)(O)OCC2C(C(C(O2)N3C=CC(=O)NC3=O)O)O)CO)O)O
CACTVS 3.341CC(=O)N[CH]1[CH](O)[CH](O)[CH](CO)O[CH]1O[P](O)(=O)O[P](O)(=O)OC[CH]2O[CH]([CH](O)[CH]2O)N3C=CC(=O)NC3=O
ACDLabs 10.04O=P(OC1OC(C(O)C(O)C1NC(=O)C)CO)(O)OP(=O)(O)OCC3OC(N2C=CC(=O)NC2=O)C(O)C3O
CACTVS 3.341CC(=O)N[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[P@](O)(=O)O[P@](O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N3C=CC(=O)NC3=O
OpenEye OEToolkits 1.5.0CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]2[C@H]([C@H]([C@@H](O2)N3C=CC(=O)NC3=O)O)O)CO)O)O
FormulaC17 H27 N3 O17 P2
NameURIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE
ChEMBLCHEMBL388154
DrugBankDB03397
ZINCZINC000008551100
PDB chain3upk Chain A Residue 427 [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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PDB3upk Functional Consequence of Covalent Reaction of Phosphoenolpyruvate with UDP-N-acetylglucosamine 1-Carboxyvinyltransferase (MurA).
Resolution2.0 Å
Binding residue
(original residue number in PDB)		N23 W95 R120 P121 V122 D123 L124 K160 S162 V163 G164 T304 D305 F328
Binding residue
(residue number reindexed from 1)		N23 W95 R120 P121 V122 D123 L124 K160 S162 V163 G164 T304 D305 F328
Annotation score3
Binding affinityPDBbind-CN: -logKd/Ki=4.30,Kd=50uM
Enzymatic activity
Catalytic site (original residue number in PDB) K22 N23 D49 R91 C115 R120 D305 H334 L370 R371 R397
Catalytic site (residue number reindexed from 1) K22 N23 D49 R91 C115 R120 D305 H334 L370 R371 R397
Enzyme Commision number 2.5.1.7: UDP-N-acetylglucosamine 1-carboxyvinyltransferase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008760 UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
GO:0016740 transferase activity
GO:0016765 transferase activity, transferring alkyl or aryl (other than methyl) groups
Biological Process
GO:0008360 regulation of cell shape
GO:0009252 peptidoglycan biosynthetic process
GO:0019277 UDP-N-acetylgalactosamine biosynthetic process
GO:0051301 cell division
GO:0071555 cell wall organization
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3upk, PDBe:3upk, PDBj:3upk
PDBsum3upk
PubMed22378791
UniProtP33038|MURA_ENTCC UDP-N-acetylglucosamine 1-carboxyvinyltransferase (Gene Name=murA)

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