Zn-binding domain of the T347G mutant of human aminoacylase-I
The structure was published by Lindner, H.A., Lunin, V.V., Alary, A., Hecker, R., Cygler, M., and Menard, R., in 2003 in a paper entitled "Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.4 Å and deposited in 2003.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely Aminoacylase-1.
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 has more than one probable quaternary state observed. For more details see the quaternary structure page.
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: