Q6VAB6: Kinase suppressor of Ras 2 (KSR2)

Kinase suppressor of Ras 2 (KSR2) is a 950-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q6VAB6.

Gene
KSR2
Organism
Homo sapiens
Length
950 residues
Mean pLDDT
60.8
Model
AF-Q6VAB6-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 60.8 (low overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate20%
70 to 90Confident: backbone generally right26%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions49%

What pLDDT means and how to read it

Function

Location-regulated scaffold connecting MEK to RAF. Has very low protein kinase activity and can phosphorylate MAP2K1 at several Ser and Thr residues with very low efficiency (in vitro). Acts as MAP2K1/MEK1-dependent allosteric activator of BRAF; upon binding to MAP2K1/MEK1, dimerizes with BRAF and promotes BRAF-mediated phosphorylation of MAP2K1/MEK1 (PubMed:29433126). Interaction with BRAF enhances KSR2-mediated phosphorylation of MAP2K1 (in vitro). Blocks MAP3K8 kinase activity and MAP3K8-mediated signaling. Acts as a negative regulator of MAP3K3-mediated activation of ERK, JNK and NF-kappa-B pathways, inhibiting MAP3K3-mediated interleukin-8 production

Subunit structure

Heterodimerizes (via N-terminus) with BRAF (via N-terminus) in a MAP2K1/MEK1-dependent manner (PubMed:29433126). Interacts with BRAF; this increases the low intrinsic protein kinase activity of KSR2 (PubMed:21441910). Interacts with MAP2K1, forming a heterodimer that can dimerize to form a heterotetramer (PubMed:12975377, PubMed:21441910, PubMed:29433126). Interacts with MAP3K8, MAPK, RAS and…

Subcellular location

Cytoplasm, Membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
7JURX-ray2.82 ÅB=634-950
7JUSX-ray2.99 ÅB=634-950
7JUTX-ray3.09 ÅB=634-950
7JUUX-ray3.19 ÅB=634-950
7JUQX-ray3.22 ÅB=634-950
7UMBX-ray3.23 ÅB=634-950
7JUVX-ray3.36 ÅB=634-950
2Y4IX-ray3.46 ÅB=634-950
5KKRX-ray3.51 ÅB=634-950

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