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PDB: 8 results

3TWD
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BU of 3twd by Molmil
glmuC1 in complex with an antibacterial inhibitor
Descriptor: 4-({5-[(4-aminophenyl)(phenyl)sulfamoyl]-2,4-dimethoxyphenyl}amino)-4-oxobutanoic acid, Bifunctional protein glmU, SULFATE ION
Authors:Lahiri, S, Otterbein, L.
Deposit date:2011-09-21
Release date:2011-10-19
Last modified:2024-02-28
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:In Vitro Validation of Acetyltransferase Activity of GlmU as an Antibacterial Target in Haemophilus influenzae.
J.Biol.Chem., 286, 2011
4AA7
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BU of 4aa7 by Molmil
E.coli GlmU in complex with an antibacterial inhibitor
Descriptor: BIFUNCTIONAL PROTEIN GLMU, N-(2,4-dimethoxy-5-{[(2R)-2-methyl-2,3-dihydro-1H-indol-1-yl]sulfonyl}phenyl)acetamide, SULFATE ION
Authors:Otterbein, L, Breed, J, Ogg, D.J.
Deposit date:2011-11-30
Release date:2012-08-15
Last modified:2023-12-20
Method:X-RAY DIFFRACTION (2 Å)
Cite: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.
Bioorg.Med.Chem.Lett., 22, 2012
1HV9
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STRUCTURE OF E. COLI GLMU: ANALYSIS OF PYROPHOSPHORYLASE AND ACETYLTRANSFERASE ACTIVE SITES
Descriptor: COBALT (II) ION, COENZYME A, UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE, ...
Authors:Olsen, L.R, Roderick, S.L.
Deposit date:2001-01-08
Release date:2001-02-21
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites.
Biochemistry, 40, 2001
2OI6
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E. coli GlmU- Complex with UDP-GlcNAc, CoA and GlcN-1-PO4
Descriptor: 2-amino-2-deoxy-1-O-phosphono-alpha-D-glucopyranose, Bifunctional protein glmU, COBALT (II) ION, ...
Authors:Olsen, L.R, Vetting, M.W, Roderick, S.L.
Deposit date:2007-01-10
Release date:2007-06-19
Last modified:2023-08-30
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products.
Protein Sci., 16, 2007
1FXJ
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BU of 1fxj by Molmil
CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE
Descriptor: 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, SULFATE ION, UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE
Authors:Brown, K, Pompeo, F, Dixon, S, Mengin-Lecreulx, D, Cambillau, C, Bourne, Y.
Deposit date:2000-09-26
Release date:2000-10-18
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.25 Å)
Cite:Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily.
EMBO J., 18, 1999
2OI5
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BU of 2oi5 by Molmil
E. coli GlmU- Complex with UDP-GlcNAc and Acetyl-CoA
Descriptor: ACETYL COENZYME *A, Bifunctional protein glmU, MAGNESIUM ION, ...
Authors:Olsen, L.R, Vetting, M.W, Roderick, S.L.
Deposit date:2007-01-10
Release date:2007-06-19
Last modified:2023-08-30
Method:X-RAY DIFFRACTION (2.25 Å)
Cite:Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products.
Protein Sci., 16, 2007
1FWY
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BU of 1fwy by Molmil
CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE BOUND TO UDP-GLCNAC
Descriptor: 1,2-ETHANEDIOL, SULFATE ION, UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE, ...
Authors:Brown, K, Pompeo, F, Dixon, S, Mengin-Lecreulx, D, Cambillau, C, Bourne, Y.
Deposit date:2000-09-25
Release date:2000-10-18
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily.
EMBO J., 18, 1999
2OI7
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BU of 2oi7 by Molmil
E. coli GlmU- Complex with UDP-GlcNAc, desulpho-CoA and GlcNAc-1-PO4
Descriptor: 2-acetamido-2-deoxy-1-O-phosphono-alpha-D-glucopyranose, Bifunctional protein glmU, COBALT (II) ION, ...
Authors:Olsen, L.R, Vetting, M.W, Roderick, S.L.
Deposit date:2007-01-10
Release date:2007-06-19
Last modified:2023-08-30
Method:X-RAY DIFFRACTION (2.54 Å)
Cite:Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products.
Protein Sci., 16, 2007

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