Structure of PDB 4kql Chain A Binding Site BS01

Receptor Information
>4kql Chain A (length=450) Species: 727 (Haemophilus influenzae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KALSAVILAAGKGTRMYSDLPKVLHTIAGKPMVKHVIDTAHQLGSENIHL
IYGHGGDLMRTHLANEQVNWVLQTEQLGTAHAVQQAAPFFKDNENIVVLY
GDAPLITKETLEKLIEAKPENGIALLTVNLDNPTGYGRIIRENGNVVAIV
EQKDANAEQLNIKEVNTGVMVSDGASFKKWLARVGNNNAQGEYYLTDLIA
LANQDNCQVVAVQATDVMEVEGANNRLQLAALERYFQNKQASKLLLEGVM
IYDPARFDLRGTLEHGKDVEIDVNVIIEGNVKLGDRVKIGTGCVLKNVVI
GNDVEIKPYSVLEDSIVGEKAAIGPFSRLRPGAELAAETHVGNFVEIKKS
TVGKGSKVNHLTYVGDSEIGSNCNIGAGVITCNYDGANKFKTIIGDDVFV
GSDTQLVAPVKVANGATIGAGTTITRDVGENELVITRVAQRHIQGWQRPI
Ligand information
Ligand ID1SG
InChIInChI=1S/C24H19N5O5/c1-34-18-11-14(19-13-26-24(33)29-22(19)31)10-15(12-18)21(30)27-16-5-7-17(8-6-16)28-23(32)20-4-2-3-9-25-20/h2-13H,1H3,(H,27,30)(H,28,32)(H2,26,29,31,33)
InChIKeyIDGYBMGDEPAAQL-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.370COc1cc(cc(c1)C2=CNC(=O)NC2=O)C(=O)Nc3ccc(NC(=O)c4ccccn4)cc3
OpenEye OEToolkits 1.7.6COc1cc(cc(c1)C(=O)Nc2ccc(cc2)NC(=O)c3ccccn3)C4=CNC(=O)NC4=O
ACDLabs 12.01O=C4C(c3cc(C(=O)Nc2ccc(NC(=O)c1ncccc1)cc2)cc(OC)c3)=CNC(=O)N4
FormulaC24 H19 N5 O5
NameN-(4-{[3-(2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-5-methoxybenzoyl]amino}phenyl)pyridine-2-carboxamide
ChEMBLCHEMBL3341771
DrugBank
ZINCZINC000212413307
PDB chain4kql Chain A Residue 511 [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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PDB4kql Rational design of inhibitors of the bacterial cell wall synthetic enzyme GlmU using virtual screening and lead-hopping.
Resolution2.31 Å
Binding residue
(original residue number in PDB)		A12 A13 Q76 Q79 G81 T82 Y103 D105 Y139 T170 V223 G225
Binding residue
(residue number reindexed from 1)		A9 A10 Q73 Q76 G78 T79 Y100 D102 Y136 T167 V220 G222
Annotation score1
Binding affinityMOAD: ic50=0.0017uM
PDBbind-CN: -logKd/Ki=8.77,IC50=0.0017uM
Enzymatic activity
Catalytic site (original residue number in PDB) R18
Catalytic site (residue number reindexed from 1) R15
Enzyme Commision number 2.3.1.157: glucosamine-1-phosphate N-acetyltransferase.
2.7.7.23: UDP-N-acetylglucosamine diphosphorylase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003977 UDP-N-acetylglucosamine diphosphorylase activity
GO:0016740 transferase activity
GO:0016746 acyltransferase activity
GO:0016779 nucleotidyltransferase activity
GO:0019134 glucosamine-1-phosphate N-acetyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0000902 cell morphogenesis
GO:0006048 UDP-N-acetylglucosamine biosynthetic process
GO:0008360 regulation of cell shape
GO:0009245 lipid A biosynthetic process
GO:0009252 peptidoglycan biosynthetic process
GO:0071555 cell wall organization
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4kql, PDBe:4kql, PDBj:4kql
PDBsum4kql
PubMed25262942
UniProtP43889|GLMU_HAEIN Bifunctional protein GlmU (Gene Name=glmU)

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