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PDBe Entry: 1p43 view

REVERSE PROTONATION IS THE KEY TO GENERAL ACID-BASE CATALYSIS IN ENOLASE
Summary
Header LYASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.8 Å, R-factor: 18.5%, Free R-factor: 21.3%, Spacegroup: P 21 21 2
Released 18/11/2003, deposition: 21/04/2003, last revision: 24/02/2009
Authors Sims, P.A.search; Larsen, T.M.search; Poyner, R.R.search; Cleland, W.W.search; Reed, G.H.search
Primary citation Reverse protonation is the key to general acid-base catalysis in enolase
BIOCHEMISTRYsearch vol:42, pag:8298-8306 (2003) [PubMed ID 12846578 ]search
Keywords Beta Barrelsearch, LYASEsearch
EC 4.2.1.11 ExPASy BRENDA search (A B)
Organism Saccharomyces cerevisiae(baker's yeast) 4932search(A B)
UniProt Enolase 1 (EC 4.2.1.11) (2-phosphoglycerate dehydratase 1) (2-phospho-D-glycerate hydro-lyase 1) P00924search (A B)
Solvent A, B
Related entries 1p48
Polymers
Id Name Type UniProt Residues Observed
A, B Enolase 1 Protein P00924 (ENO1_YEAST)search
436 100%
Heterogens
Id Name Ligands
A, B MAGNESIUM ION MG search
A, B 2-PHOSPHOGLYCERIC ACID 2PG search
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