P87074: DNA repair protein crb2 (crb2)

DNA repair protein crb2 (crb2) is a 778-residue protein from Schizosaccharomyces pombe (strain 972 / ATCC 24843). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P87074.

Gene
crb2
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Length
778 residues
Mean pLDDT
63.3
Model
AF-P87074-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 63.3 (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 accurate32%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions49%

What pLDDT means and how to read it

Function

Essential for cell cycle arrest at the G1 and G2 stages following DNA damage by X-, and UV-irradiation, or inactivation of DNA ligase. Plays a role in the response to DNA damage (PubMed:9153313, PubMed:9407031). Interaction with rad4 via its phosphorylation sites in the N-terminus couples the DNA checkpoint apparatus to chromatin via interaction of its C-terminal BRCT domains with epigenetic modifications on histones H4 and H2A, respectively, in the G1/S phase of the cell cycle, and facilitates recruitment of the checkpoint kinase chk1 (PubMed:15550243, PubMed:16778077, PubMed:18826944, PubMed:20679485, PubMed:22792081)

Subunit structure

Homodimer. Dimerization is mediated via the BRCT domain (PubMed:16778077, PubMed:18676809). Interacts (via BRCT domain) with rad3 (PubMed:14739927). Interacts with rad4 (via BRCT1,2 domains) (PubMed:9407031, PubMed:14739927); a single rad4 molecule interacts simultaneously with both Thr-187 phosphorylation sites in a crb2 dimer (PubMed:24074952). Interacts (via Tudor domain) with histone…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4BU0X-ray1.5 ÅB/C=180-193
4BU1X-ray2.1 ÅC/D=229-241
2VXBX-ray2.3 ÅA/B=538-778
2FHDX-ray2.4 ÅA/B/C=358-507
2VXCX-ray3.1 ÅA/B=537-778

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