Q2M1P5: Kinesin-like protein KIF7 (KIF7)

Kinesin-like protein KIF7 (KIF7) is a 1343-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q2M1P5.

Gene
KIF7
Organism
Homo sapiens
Length
1343 residues
Mean pLDDT
67.2
Model
AF-Q2M1P5-F1 v6
Model created
1 Aug 2025
PDB structures
5

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 67.2 (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 accurate17%
70 to 90Confident: backbone generally right44%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions28%

What pLDDT means and how to read it

Function

Essential for hedgehog signaling regulation: acts both as a negative and positive regulator of sonic hedgehog (Shh) and Indian hedgehog (Ihh) pathways, acting downstream of SMO, through both SUFU-dependent and -independent mechanisms (PubMed:21633164). Involved in the regulation of microtubular dynamics. Required for proper organization of the ciliary tip and control of ciliary localization of SUFU-GLI2 complexes (By similarity). Required for localization of GLI3 to cilia in response to Shh. Negatively regulates Shh signaling by preventing inappropriate activation of the transcriptional activator GLI2 in the absence of ligand. Positively regulates Shh signaling by preventing the processing…

Subunit structure

Can form homodimers and interacts with microtubules (By similarity). Interacts with GLI1, GLI2, GLI3, SMO and SUFU (PubMed:19592253). Interacts with NPHP1 (PubMed:21633164). Interacts with SMO and DLG5 (via PDZ4 or guanylate kinase-like domain) (By similarity)

Subcellular location

Cell projection, cilium, Cytoplasm, cytoskeleton, cilium basal body

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4A14X-ray1.6 ÅA=8-347
2XT3X-ray1.88 ÅA=8-347
7RX0EM3.89 ÅC=1-543
6MLQEM4.2 ÅC=1-398
6MLREM4.2 ÅC=1-398

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.