T. MARITIMA ADENYLOSUCCINATE LYASE
The structure was published by Toth, E.A. and Yeates, T.O., in 2000 in a paper entitled "The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1999.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of PROTEIN (ADENYLOSUCCINATE LYASE).
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: