1EBG

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

Summary for 1EBG

Entry DOI	10.2210/pdb1ebg/pdb
Descriptor	ENOLASE, MAGNESIUM ION, PHOSPHONOACETOHYDROXAMIC ACID, ... (4 entities in total)
Functional Keywords	carbon-oxygen lyase
Biological source	Saccharomyces cerevisiae (baker's yeast)
Cellular location	Cytoplasm: P00924
Total number of polymer chains	2
Total formula weight	93872.91
Authors	Wedekind, J.E.,Reed, G.H.,Rayment, I. (deposition date: 1994-04-27, release date: 1995-04-27, Last modification date: 2024-02-07)
Primary citation	Wedekind, J.E.,Poyner, R.R.,Reed, G.H.,Rayment, I. Chelation of serine 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-A resolution. Biochemistry, 33:9333-9342, 1994 Cited by PubMed: 8049235 DOI: 10.1021/bi00197a038 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.1 Å)

Structure validation