Search Count: 4
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Reverse Protonation Is The Key To General Acid-Base Catalysis In Enolase
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION Resolution:1.80 Å Release Date: 2003-11-18 Classification: LYASE Ligands: MG, 2PG |
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION
Release Date: 2003-11-18
Ligands: MG, 2PG
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Reverse Protonation Is The Key To General Acid-Base Catalysis In Enolase
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION Resolution:2.00 Å Release Date: 2003-11-18 Classification: LYASE Ligands: MG, PEP |
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION
Release Date: 2003-11-18
Ligands: MG, PEP
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Mg-Phosphonoacetohydroxamate Complex Of S39A Yeast Enolase 1
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION Resolution:2.10 Å Release Date: 2002-04-03 Classification: LYASE Ligands: MG, PAH |
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION
Release Date: 2002-04-03
Ligands: MG, PAH
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Chelation Of Ser 39 To Mg2+ Latches A Gate At The Active Site Of Enolase: Structure Of The Bis(Mg2+) Complex Of Yeast Enolase And The Intermediate Analog Phosphonoacetohydroxamate At 2.1 Angstroms Resolution
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION Resolution:2.10 Å Release Date: 1995-04-27 Classification: CARBON-OXYGEN LYASE Ligands: MG, PAH |
Organism: Saccharomyces cerevisiae
Method: X-RAY DIFFRACTION
Release Date: 1995-04-27
Ligands: MG, PAH