NOVEL AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE MAKE SELECTIVE INTERACTIONS WITH CONSERVED RESIDUES AND WATER MOLECULES IN THE ACTIVE SITE
The structure was published by Finley, J.B., Atigadda, V.R., Duarte, F., et al., Brouillette, W.J., Air, G.M., and Luo, M., in 1999 in a paper entitled "Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1999.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of PROTEIN (NEURAMINIDASE). This molecule has the UniProt identifier P03474 (NRAM_INBLE). The sample contained 390 residues which is < 90% of the natural sequence. Out of 390 residues 390 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 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: