Structure of PDB 4aa7 Chain A

Receptor sequence
>4aa7A (length=222) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
LSRLERVYQSEQAEKLLLAGVMLRDPARFDLRGTLTHGRDVEIDTNVIIE
GNVTLGHRVKIGTGCVIKNSVIGDDCEISPYTVVEDANLAAACTIGPFAR
LRPGAELLEGAHVGNFVEMKKARLGKGSKAGHLTYLGDAEIGDNVNIGAG
TITCNYDGANKFKTIIGDDVFVGSDTQLVAPVTVGKGATIAAGTTVTRNV
GENALAISRVPQTQKEGWRRPV
3D structure
PDB4aa7 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.
ChainA
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.1.157: glucosamine-1-phosphate N-acetyltransferase.
2.7.7.23: UDP-N-acetylglucosamine diphosphorylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 R82 A C385 Y387 D388 V410 C154 Y156 D157 V179 MOAD: ic50=2uM
PDBbind-CN: -logKd/Ki=5.70,IC50=2uM
BindingDB: IC50=2000nM
Gene Ontology
Molecular Function
GO:0003977 UDP-N-acetylglucosamine diphosphorylase activity
GO:0016740 transferase activity
GO:0019134 glucosamine-1-phosphate N-acetyltransferase activity
Biological Process
GO:0006048 UDP-N-acetylglucosamine biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4aa7, PDBe:4aa7, PDBj:4aa7
PDBsum4aa7
PubMed22297115
UniProtP0ACC7|GLMU_ECOLI Bifunctional protein GlmU (Gene Name=glmU)

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