2y4i Summary

pdbe.org/2y4i
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KSR2-MEK1 HETERODIMER

The structure was published by Brennan, D.F., Dar, A.C., Hertz, N.T., et al., Burlingame, A.L., Shokat, K.M., and Barford, D., in 2011 in a paper entitled "A Raf-Induced Allosteric Transition of Ksr Stimulates Ksr and Raf Phosphorylation of Mek" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.46 Å and deposited in 2011.

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

This PDB entry contains a complex of 2 biomacromolecules, namely KINASE SUPPRESSOR OF RAS 2 and DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 1.

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 heterodimers.

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
B KINASE SUPPRESSOR OF RAS 2 Q6VAB6 (634-950) (KSR2_HUMAN)search Homo sapienssearch < 90% 319 83%
C DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 1 P29678 (1-393) (MP2K1_RABIT)search Oryctolagus cuniculussearch 100% 395 79%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
Q6VAB6 (634 - 950) KINASE SUPPRESSOR OF RAS 2 Homo sapiens
P29678 (1 - 393) DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 1 Oryctolagus cuniculus

Chain Structural classification (CATH) Sequence family (Pfam)
B Phosphorylase Kinase; domain 1search Protein tyrosine kinasesearch
C (P29678) PF00069: Protein kinase domainsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
B (Q6VAB6) transferase activity, transferring phosphorus-containing groupssearch protein kinase activitysearch ATP bindingsearch protein serine/threonine kinase activitysearch protein phosphorylationsearch
C (P29678) protein kinase activitysearch ATP bindingsearch protein serine/threonine kinase activitysearch transferase activity, transferring phosphorus-containing groupssearch protein tyrosine kinase activitysearch transferase activitysearch nucleotide bindingsearch kinase activitysearch protein phosphorylationsearch peptidyl-tyrosine phosphorylationsearch phosphorylationsearch cytoplasmsearch microtubule organizing centersearch cytoskeletonsearch nucleussearch

Chain InterPro annotation
B Protein kinase domainsearch Serine-threonine/tyrosine-protein kinase catalytic domainsearch Serine/threonine-protein kinase, active sitesearch Protein kinase-like domainsearch
C Protein kinase domainsearch Serine/threonine/dual specificity protein kinase, catalytic domainsearch Serine/threonine-protein kinase, active sitesearch Protein kinase-like domainsearch Protein kinase, ATP binding sitesearch