Q9HAW4: Claspin (CLSPN)

Claspin (CLSPN) is a 1339-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9HAW4.

Gene
CLSPN
Organism
Homo sapiens
Length
1339 residues
Mean pLDDT
50.6
Model
AF-Q9HAW4-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 50.6 (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 accurate7%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution14%
Below 50Very low: often disordered regions60%

What pLDDT means and how to read it

Function

Required for checkpoint mediated cell cycle arrest in response to inhibition of DNA replication or to DNA damage induced by both ionizing and UV irradiation (PubMed:12766152, PubMed:15190204, PubMed:15707391, PubMed:16123041). Adapter protein which binds to BRCA1 and the checkpoint kinase CHEK1 and facilitates the ATR-dependent phosphorylation of both proteins (PubMed:12766152, PubMed:15096610, PubMed:15707391, PubMed:16123041). Also required to maintain normal rates of replication fork progression during unperturbed DNA replication. Binds directly to DNA, with particular affinity for branched or forked molecules and interacts with multiple protein components of the replisome such as the…

Subunit structure

Interacts (phosphorylation-dependent) with CHEK1; regulates CLSPN function in checkpoint for DNA damage and replication (PubMed:12766152, PubMed:15707391, PubMed:16963448). Interacts with ATR and RAD9A and these interactions are slightly reduced during checkpoint activation (PubMed:12766152). Interacts with BRCA1 and this interaction increases during checkpoint activation (PubMed:15096610).…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9TDZX-ray1.35 ÅB=26-37
7AKOX-ray1.8 ÅC/D=937-952
7PLOEM2.8 ÅQ=1-1339
7PFOEM3.2 ÅQ=1-1339
8B9DEM3.4 ÅQ=1-1339

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