2f9g Summary


Crystal structure of Fus3 phosphorylated on Tyr182

The structure was published by Bhattacharyya, R.P., Remenyi, A., Good, M.C., Bashor, C.J., Falick, A.M., and Lim, W.A., in 2006 in a paper entitled "The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 2005.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of Mitogen-activated protein kinase FUS3. This molecule has the UniProt identifier P16892 (FUS3_YEAST)search. The sample contained 353 residues which is 100% of the natural sequence. Out of 353 residues 328 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):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Mitogen-activated protein kinase FUS3 P16892 (1-353) (FUS3_YEAST)search Saccharomyces cerevisiae S288csearch 100% 353 94%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P16892 (1 - 353) Mitogen-activated protein kinase FUS3 Saccharomyces cerevisiae

Chain Structural classification (CATH) Sequence family (Pfam)
A (P16892) Phosphorylase Kinase; domain 1search, Transferase(Phosphotransferase) domain 1search PF00069: Protein kinase domainsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P16892) ATP bindingsearch protein bindingsearch transferase activity, transferring phosphorus-containing groupssearch protein kinase activitysearch MAP kinase activitysearch protein serine/threonine kinase activitysearch identical protein bindingsearch nucleotide bindingsearch transferase activitysearch kinase activitysearch MAPK cascadesearch protein phosphorylationsearch pheromone-dependent signal transduction involved in conjugation with cellular fusionsearch mitotic nuclear divisionsearch invasive growth in response to glucose limitationsearch conjugationsearch negative regulation of transposition, RNA-mediatedsearch positive regulation of protein export from nucleussearch cell cycle arrestsearch cell cyclesearch cell divisionsearch phosphorylationsearch negative regulation of MAPK cascadesearch mating projection tipsearch periplasmic spacesearch nucleussearch cytoplasmsearch

Chain InterPro annotation
A Protein kinase domainsearch Serine/threonine/dual specificity protein kinase, catalytic domainsearch Mitogen-activated protein (MAP) kinase, conserved sitesearch Serine/threonine-protein kinase, active sitesearch Protein kinase-like domainsearch Protein kinase, ATP binding sitesearch