O60671: Cell cycle checkpoint protein RAD1 (RAD1)

Cell cycle checkpoint protein RAD1 (RAD1) is a 282-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O60671.

Gene
RAD1
Organism
Homo sapiens
Length
282 residues
Mean pLDDT
89.4
Model
AF-O60671-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 89.4 (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 accurate74%
70 to 90Confident: backbone generally right17%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair (PubMed:10846170, PubMed:10884395). The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex (PubMed:12578958). Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER) (PubMed:15871698). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct…

Subunit structure

Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex, composed of RAD9A, RAD1 and HUS1 (PubMed:10846170, PubMed:10884395, PubMed:31776186). The 9-1-1 complex associates with LIG1, POLB, FEN1, RAD17, HDAC1, RPA1 and RPA2 (PubMed:10846170, PubMed:10884395, PubMed:15314187, PubMed:15556996, PubMed:15871698, PubMed:15897895, PubMed:16216273). The 9-1-1 complex associates with the RAD17-RFC…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8GNNX-ray2.12 ÅC=1-282
6J8YX-ray2.4 ÅC=1-282
3A1JX-ray2.5 ÅC=13-275
8WU8X-ray2.81 ÅC=1-282
3G65X-ray2.9 ÅB=1-282
3GGRX-ray3.2 ÅC=1-282
7Z6HEM3.59 ÅB/K=1-282

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