FUMARASE MUTANT H188N WITH BOUND SUBSTRATE L-MALATE AT PUTATIVE ACTIVATOR SITE
The structure was published by Weaver, T., Lees, M., and Banaszak, L., in 1997 in a paper entitled "Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.95 Å and deposited in 1997.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of FUMARASE C.
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: