Structure of PDB 5wi5 Chain C Binding Site BS02

Receptor Information
>5wi5 Chain C (length=421) Species: 170187 (Streptococcus pneumoniae TIGR4) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MDKIVVQGGDNRLVGSVTIEGAKNAVLPLLAATILASEGKTVLQNVPILS
DVFIMNQVVGGLNAKVDFDEEAHLVKVDATGDITEEAPYKYVSKMRASIV
VLGPILARVGHAKVSMPGGCTIGSRPIDLHLKGLEAMGVKISQTAGYIEA
KAERLHGAHIYMDFPSVGATQNLMMAATLADGVTVIENAAREPEIVDLAI
LLNEMGAKVKGAGTETITITGVEKLHGTTHNVVQDRIEAGTFMVAAAMTG
GDVLIRDAVWEHNRPLIAKLLEMGVEVIEEDEGIRVRSQLENLKAVHVKT
LPHPGFPTDMQAQFTALMTVAKGESTMVETVFENRFQHLEEMRRMGLHSE
IIRDTARIVGGQPLQGAEVLSTDLRASAALILTGLVAQGETVVGKLVHLD
RGYYGFHEKLAQLGAKIQRIE
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 chain5wi5 Chain C Residue 503 [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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PDB5wi5 2.0 Angstrom Resolution Crystal Structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase from Streptococcus pneumoniae in Complex with Uridine-diphosphate-2(n-acetylglucosaminyl) butyric acid, (2R)-2-(phosphonooxy)propanoic acid and Magnesium.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		K23 N24 R125 P126 I127 D128 L129 F164 S166 V167 G168 T308 D309 V331 F332
Binding residue
(residue number reindexed from 1)		K23 N24 R125 P126 I127 D128 L129 F164 S166 V167 G168 T308 D309 V331 F332
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) K23 N24 C120 R125 D309 R401
Catalytic site (residue number reindexed from 1) K23 N24 C120 R125 D309 R401
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
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5wi5, PDBe:5wi5, PDBj:5wi5
PDBsum5wi5
PubMed
UniProtQ97NQ4|MURA1_STRPN UDP-N-acetylglucosamine 1-carboxyvinyltransferase 1 (Gene Name=murA1)

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