English Statistics Help FAQ Contact Us
Download >>

PDBj (Protein Data Bank Japan) maintains a centralized PDB archive of macromolecular structures and provides integrated tools, in collaboration with the RCSB, the BMRB in USA and the PDBe in EU. PDBj is supported by JST-NBDC and Osaka University.

Summary Structural Experimental Function Sequence Neighbor Download Link


<Asymmetric unit>
= <Biological unit>

More images...
View in 3D molecule viewer
( jV3 / Jmol ) *1
PDB ID1ebg  sequence information (FASTA format)   
DescriptorENOLASE (E.C.4.2.1.11) (2-PHOSPHO-D-GLYCERATE HYDROLASE) (APO FORM)
TitleCHELATION 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
Functional KeywordsCARBON-OXYGEN LYASE
Biological sourceSaccharomyces cerevisiae (baker's yeast)
Cellular location [UNP - P00924] Cytoplasm
Total number of polymer chains2
Total molecular weight93873.8 (the details in Structural Details Page)
AuthorsWedekind, J.E. , Reed, G.H. , Rayment, I. (deposition date : 1994-04-27, release date : 1995-04-27)
Primary citationWedekind, 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.(PubMed : 8049235)  (DOI: 10.1021/bi00197a038)
Experimental methodX-RAY DIFFRACTION ( 2.1[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P00924 ) , eF-site , KEGG ( EC 4.2.1.11 ) , PISA