Structure of PDB 3iss Chain F Binding Site BS02

Receptor Information
>3iss Chain F (length=418) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDV
DTSMKLLSQLGAKVERDGSVHIDARDVNVFCAPYDLVKTMRASIWALGPL
VARFGQGQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKASVDGR
LKGAHIVMDKVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLIT
LGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTFLVAAAISRGKII
CRNAQPDTLDAVLAKLRDAGADIEVGEDWISLDMHGKRPKAVNVRTAPHP
AFPTDMQAQFTLLNLVAEGTGFITETVFENRFMHVPELSRMGAHAEIESN
TVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYE
RIEDKLRALGANIERVKG
Ligand information
Ligand IDEPU
InChIInChI=1S/C20H29N3O19P2/c1-7(18(30)31)38-16-12(21-8(2)25)19(40-9(5-24)14(16)28)41-44(35,36)42-43(33,34)37-6-10-13(27)15(29)17(39-10)23-4-3-11(26)22-20(23)32/h3-4,9-10,12-17,19,24,27-29H,1,5-6H2,2H3,(H,21,25)(H,30,31)(H,33,34)(H,35,36)(H,22,26,32)/t9-,10-,12-,13-,14-,15-,16-,17-,19-/m1/s1
InChIKeyBEGZZYPUNCJHKP-DBYWSUQTSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CC(=O)N[CH]1[CH](O[CH](CO)[CH](O)[CH]1OC(=C)C(O)=O)O[P](O)(=O)O[P](O)(=O)OC[CH]2O[CH]([CH](O)[CH]2O)N3C=CC(=O)NC3=O
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)OC(=C)C(=O)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)OC(=C)C(=O)O
ACDLabs 10.04O=P(OC1OC(C(O)C(O/C(=C)C(=O)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](CO)[C@@H](O)[C@@H]1OC(=C)C(O)=O)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
FormulaC20 H29 N3 O19 P2
NameURIDINE-DIPHOSPHATE-2(N-ACETYLGLUCOSAMINYL) BUTYRIC ACID;
ENOLPYRUVYL-URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE
ChEMBL
DrugBank
ZINCZINC000024684039
PDB chain3iss Chain F Residue 606 [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]
PDB3iss Evidence of Kinetic Control of Ligand Binding and Staged Product Release in MurA (Enolpyruvyl UDP-GlcNAc Synthase)-Catalyzed Reactions .
Resolution2.5 Å
Binding residue
(original residue number in PDB)		K22 N23 P121 V122 D123 L124 K160 S162 V163 G164 D305 F328
Binding residue
(residue number reindexed from 1)		K22 N23 P121 V122 D123 L124 K160 S162 V163 G164 D305 F328
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) K22 N23 D49 A92 C115 R120 H299 D305 E325 L370 R371 R397
Catalytic site (residue number reindexed from 1) K22 N23 D49 A92 C115 R120 H299 D305 E325 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
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3iss, PDBe:3iss, PDBj:3iss
PDBsum3iss
PubMed19899805
UniProtP0A749|MURA_ECOLI UDP-N-acetylglucosamine 1-carboxyvinyltransferase (Gene Name=murA)

[Back to BioLiP]