Inosine-Adenosine-Guanosine Preferring Nucleoside Hydrolase From Trypanosoma vivax: Trp260Ala Mutant In Complex With 3-Deaza-Adenosine
The structure was published by Versees, W., Loverix, S., Vandemeulebroucke, A., Geerlings, P., and Steyaert, J., in 2004 in a paper entitled "Leaving group activation by aromatic stacking: an alternative to general Acid catalysis." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 2003.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of IAG-nucleoside hydrolase.
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: