Brand  (β version)

PDB ID: 4E1K

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Ligands
Code Name Style Show Link
0N5 N-{4-[(7-hydroxy-6-methoxyquinazolin-4-yl)amino]phenyl}benzamide PoSSuM
PG4 Tetraethylene glycol PoSSuM
SO4 Sulfate ion PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 4E1K   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE/TRANSFERASE INHIBITOR
Title : GlmU in complex with a Quinazoline Compound
Release Data : 2013-05-29
Compound :
mol_id molecule chains synonym
1 Bifunctional protein GlmU A UDP-N-acetylglucosamine pyrophosphorylase, N-acetylglucosamine-1-phosphate uridyltransferase, Glucosamine-1-phosphate N-acetyltransferase
ec: 2.7.7.23, 2.3.1.157
Source :
mol_id organism_scientific expression_system
1 Haemophilus influenzae  (taxid:71421) Escherichia coli  (taxid:562)
strain: ATCC 51907 / DSM 11121 / KW20 / Rd
gene: glmU, HI_0642
Authors : Larsen, N.A., Doig, P.
Keywords : peptidoglycan synthesis, cell shape, metal-binding, cell wall biogenesis/degradation, multifunctional enzyme, acyltransferase, uridyltransferase, Nucleotidyl transferase, TRANSFERASE-TRANSFERASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 2.00 Å )
Citation :

An aminoquinazoline inhibitor of the essential bacterial cell wall synthetic enzyme GlmU has a unique non-protein-kinase-like binding mode.

Larsen, N.A.,Nash, T.J.,Morningstar, M.  et al.
(2012)  Biochem.J.  446 : 405 - 413

PubMed: 22721802
DOI: 10.1042/BJ20120596

Reaction

Chain : A
UniProt : P43889 (GLMU_HAEIN)
Reaction: EC: Evidence:
Physiological Direction:
alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha- D-glucosamine 1-phosphate + CoA + H(+) 2.3.1.157 HAMAP-Rule:MF_01631
-
N-acetyl-alpha-D-glucosamine 1-phosphate + UTP + H(+) = UDP-N- acetyl-alpha-D-glucosamine + diphosphate 2.7.7.23 HAMAP-Rule:MF_01631
-
Cofactor: Evidence: Note:
Mg(2+) ECO:0000255 | HAMAP-Rule:MF_01631
Binds 1 Mg(2+) ion per subunit.