CONTRIBUTION OF THE ACTIVE SITE ASPARTIC ACID TO CATALYSIS IN THE BACTERIAL NEURAMINIDASE FROM MICROMONOSPORA VIRIDIFACIENS
The structure was published by Watson, J.N., Newstead, S., Dookhun, V., Taylor, G., and Bennet, A.J., in 2004 in a paper entitled "Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora Viridifaciens" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 2004.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of BACTERIAL SIALIDASE. This molecule has the UniProt identifier Q02834 (NANH_MICVI). The sample contained 601 residues which is 99% of the natural sequence. Out of 601 residues 601 were observed and are deposited in the PDB.
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 is most likely monomeric.
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: