Structure of PDB 4knr Chain A Binding Site BS01

Receptor Information
>4knr 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 ID1S8
InChIInChI=1S/C29H24N4O3/c1-36-26-17-23-24(18-25(26)34)32-27(16-19-8-4-2-5-9-19)33-28(23)30-21-12-14-22(15-13-21)31-29(35)20-10-6-3-7-11-20/h2-15,17-18,34H,16H2,1H3,(H,31,35)(H,30,32,33)
InChIKeyMWYUDSZCUZWZIP-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6COc1cc2c(cc1O)nc(nc2Nc3ccc(cc3)NC(=O)c4ccccc4)Cc5ccccc5
CACTVS 3.370COc1cc2c(Nc3ccc(NC(=O)c4ccccc4)cc3)nc(Cc5ccccc5)nc2cc1O
ACDLabs 12.01O=C(c1ccccc1)Nc2ccc(cc2)Nc4nc(nc3c4cc(OC)c(O)c3)Cc5ccccc5
FormulaC29 H24 N4 O3
NameN-{4-[(2-benzyl-7-hydroxy-6-methoxyquinazolin-4-yl)amino]phenyl}benzamide
ChEMBLCHEMBL3343036
DrugBank
ZINCZINC000263620770
PDB chain4knr Chain A Residue 501 [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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PDB4knr Rational design of inhibitors of the bacterial cell wall synthetic enzyme GlmU using virtual screening and lead-hopping.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		L11 A12 A13 G14 T82 Y103 D105 Y139 V223
Binding residue
(residue number reindexed from 1)		L8 A9 A10 G11 T79 Y100 D102 Y136 V220
Annotation score1
Binding affinityMOAD: ic50=1.8uM
PDBbind-CN: -logKd/Ki=5.74,IC50=1.8uM
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
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Cellular Component
External links
PDB RCSB:4knr, PDBe:4knr, PDBj:4knr
PDBsum4knr
PubMed25262942
UniProtP43889|GLMU_HAEIN Bifunctional protein GlmU (Gene Name=glmU)

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