Crystal Structure of endo-neuraminidaseNF
The structure was published by Schulz, E.C., Schwarzer, D., Frank, M., et al., Dickmanns, A., Gerardy-Schahn, R., and Ficner, R., in 2010 in a paper entitled "Structural basis for the recognition and cleavage of polysialic acid by the bacteriophage K1F tailspike protein EndoNF." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.41 Å and deposited in 2009.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Endo-N-acetylneuraminidase. This molecule has the UniProt identifier Q04830 (ENAN_BPK1F). The sample contained 670 residues which is < 90% of the natural sequence. Out of 670 residues 670 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 most likely forms homotrimers.
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: