Structure of PDB 4aaw Chain A Binding Site BS01

Receptor Information
>4aaw Chain A (length=455) Species: 1313 (Streptococcus pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SNFAIILAAGKGTRMKSDLPKVLHKVAGISMLEHVFRSVGAIQPEKTVTV
VGHKAELVEEVLAEQTEFVTQSEQLGTGHAVMMTEPILEGLSGHTLVIAG
DTPLITGESLKNLIDFHINHKNVATILTAETDNPFGYGRIVRNDNAEVLR
IVEQKDATDFEKQIKEINTGTYVFDNERLFEALKNINTNNEYYITDVIGI
FRETGEKVGAYTLKDFDESLGVNDRVALATAESVMRRRINHKHMVNGVSF
VNPEATYIDIDVEIAPEVQIEANVILKGQTKIGAETVLTNGTYVVDSTIG
AGAVITNSMIEESSVADGVTVGPYAHIRPNSSLGAQVHIGNFVEVKGSSI
GENTKAGHLTYIGNCEVGSNVNFGAGTITVNYDGKNKYKTVIGDNVFVGS
NSTIIAPVELGDNSLVGAGSTITKDVPADAIAIGRGRQINKDEYATRLPH
HPKNQ
Ligand information
Ligand IDR84
InChIInChI=1S/C29H37N3O11S/c1-41-23-16-24(42-2)25(15-21(23)31-26(33)7-8-27(34)35)44(39,40)30-17-20-5-3-4-6-22(20)32-13-11-19(12-14-32)18-43-29(38)10-9-28(36)37/h3-6,15-16,19,30H,7-14,17-18H2,1-2H3,(H,31,33)(H,34,35)(H,36,37)
InChIKeyPRDHHOYRFMTLDT-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385COc1cc(OC)c(cc1NC(=O)CCC(O)=O)[S](=O)(=O)NCc2ccccc2N3CCC(CC3)COC(=O)CCC(O)=O
ACDLabs 12.01O=C(O)CCC(=O)Nc1cc(c(OC)cc1OC)S(=O)(=O)NCc2ccccc2N3CCC(CC3)COC(=O)CCC(=O)O
OpenEye OEToolkits 1.9.2COc1cc(c(cc1NC(=O)CCC(=O)O)S(=O)(=O)NCc2ccccc2N3CCC(CC3)COC(=O)CCC(=O)O)OC
FormulaC29 H37 N3 O11 S
Name4-{[1-(2-{[({5-[(3-carboxypropanoyl)amino]-2,4-dimethoxyphenyl}sulfonyl)amino]methyl}phenyl)piperidin-4-yl]methoxy}-4-oxobutanoic acid
ChEMBLCHEMBL1951184
DrugBank
ZINCZINC000073279645
PDB chain4aaw Chain A Residue 1460 [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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PDB4aaw Inhibitors of Acetyltransferase Domain of N-Acetylglucosamine-1-Phosphate-Uridyltransferase/ Glucosamine-1-Phosphate-Acetyltransferase (Glmu). Part 1: Hit to Lead Evaluation of a Novel Arylsulfonamide Series.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		V384 Y386 D387 I409
Binding residue
(residue number reindexed from 1)		V380 Y382 D383 I405
Annotation score1
Binding affinityMOAD: ic50=0.5uM
PDBbind-CN: -logKd/Ki=6.30,IC50=0.5uM
Enzymatic activity
Catalytic site (original residue number in PDB) R15
Catalytic site (residue number reindexed from 1) R14
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:0009058 biosynthetic process
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:4aaw, PDBe:4aaw, PDBj:4aaw
PDBsum4aaw
PubMed22297115
UniProtQ8DQ18|GLMU_STRR6 Bifunctional protein GlmU (Gene Name=glmU)

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