CATALYTIC METAL ION BINDING IN ENOLASE: THE CRYSTAL STRUCTURE OF ENOLASE-MN2+-PHOSPHONOACETOHYDROXAMATE COMPLEX AT 2.4 ANGSTROMS RESOLUTION
The structure was published by Zhang, E., Hatada, M., Brewer, J.M., and Lebioda, L., in 1994 in a paper entitled "Catalytic metal ion binding in enolase: the crystal structure of an enolase-Mn2+-phosphonoacetohydroxamate complex at 2.4-A resolution." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 1994.
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). 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):
This entry contains 1 unique UniProt protein: