P35203: Centromere DNA-binding protein complex CBF3 subunit C (CTF13)

Centromere DNA-binding protein complex CBF3 subunit C (CTF13) is a 478-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P35203.

Gene
CTF13
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
478 residues
Mean pLDDT
78.7
Model
AF-P35203-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 78.7 (confident 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 accurate32%
70 to 90Confident: backbone generally right46%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions13%

What pLDDT means and how to read it

Function

Acts as a central component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromeres and in several promoters. The association of CBF3C with CBF3D and SGT1 is required for CBF3C activation and CBF3 assembly

Subunit structure

Component of the CBF3 complex, which is formed of CBF3A/CBF2, CBF3B/CEP3, CBF3C/CTF13 and CBF3D. CBF3C interacts with CBF3D and SGT1

Subcellular location

Nucleus, Chromosome, centromere

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6GYUEM3.0 ÅA=1-478
6GYPEM3.6 ÅA=1-478
6FE8EM3.7 ÅD=2-478
8OW1EM3.7 ÅCT=1-478
7K79EM4.0 ÅK=2-478
6GSAEM4.2 ÅD=2-478
6GYSEM4.4 ÅA/H=1-478

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