E. COLI GLUCARATE DEHYDRATASE BOUND TO XYLAROHYDROXAMATE
The structure was published by Gulick, A.M., Hubbard, B.K., Gerlt, J.A., and Rayment, I., in 2000 in a paper entitled "Evolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2000.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of GLUCARATE DEHYDRATASE.
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 homotetramers.
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: