5enl Summary

pdbe.org/5enl
spacer

INHIBITION OF ENOLASE: THE CRYSTAL STRUCTURES OF ENOLASE-CA2+-PHOSPHOGLYCERATE AND ENOLASE-ZN2+-PHOSPHOGLYCOLATE COMPLEXES AT 2.2-ANGSTROMS RESOLUTION

The structure was published by Lebioda, L., Stec, B., Brewer, J.M., and Tykarska, E., in 1991 in a paper entitled "Inhibition of enolase: the crystal structures of enolase-Ca2(+)- 2-phosphoglycerate and enolase-Zn2(+)-phosphoglycolate complexes at 2.2-A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1990.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of ENOLASE. This molecule has the UniProt identifier P00924 (ENO1_YEAST)search. The sample contained 436 residues which is 100% of the natural sequence. Out of 436 residues 436 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A ENOLASE P00924 (2-437) (ENO1_YEAST)search Saccharomyces cerevisiae S288csearch 100% 436 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00924 (2 - 437) ENOLASE Saccharomyces cerevisiae

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P00924) Enolasesearch, Enolase N-terminal domain-likesearch Enolase-like, N-terminal domainsearch, Enolase superfamilysearch PF00113: Enolase, C-terminal TIM barrel domainsearch, PF03952: Enolase, N-terminal domainsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P00924) phosphopyruvate hydratase activitysearch magnesium ion bindingsearch protein bindingsearch lyase activitysearch metal ion bindingsearch phosphopyruvate hydratase complexsearch cytoplasmsearch fungal-type vacuolesearch mitochondrionsearch glycolytic processsearch regulation of vacuole fusion, non-autophagicsearch gluconeogenesissearch

Chain InterPro annotation
A Enolasesearch Enolase, conserved sitesearch Enolase, C-terminalsearch Enolase, N-terminalsearch Enolase N-terminal domain-likesearch Enolase C-terminal domain-likesearch