Q96SD1: Protein artemis (DCLRE1C)

Protein artemis (DCLRE1C) is a 692-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96SD1.

Gene
DCLRE1C
Organism
Homo sapiens
Length
692 residues
Mean pLDDT
69.4
Model
AF-Q96SD1-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 69.4 (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 accurate46%
70 to 90Confident: backbone generally right9%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions40%

What pLDDT means and how to read it

Function

Nuclease involved in DNA non-homologous end joining (NHEJ); required for double-strand break repair and V(D)J recombination (PubMed:11336668, PubMed:11955432, PubMed:12055248, PubMed:14744996, PubMed:15071507, PubMed:15574326, PubMed:15936993). Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments (PubMed:11336668, PubMed:11955432, PubMed:14744996). V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs) (PubMed:11336668, PubMed:11955432,…

Subunit structure

Interacts with LIG4; the interaction is direct (PubMed:23219551, PubMed:23523427). Interacts with ATM (PubMed:15456891). Interacts with BRCA1 (PubMed:15456891). Interacts with PRKDC (PubMed:11955432, PubMed:14744996, PubMed:15456891, PubMed:15936993). Interacts with TP53BP1 (PubMed:15574327). Also exhibits ATM- and phosphorylation-dependent interaction with the MRN complex, composed of MRE11,…

Subcellular location

Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6TT5X-ray1.5 ÅAAA=1-361
7AFUX-ray1.56 ÅA=1-361
7AF1X-ray1.7 ÅA=1-361
7AFSX-ray1.7 ÅA=1-361
7AGIX-ray1.7 ÅA=1-361
7APVX-ray1.95 ÅA=1-361
6WO0X-ray1.97 ÅA=2-368
7ABSX-ray1.97 ÅA=2-368
4HTPX-ray2.25 ÅC/E=485-495
6WNLX-ray2.37 ÅA/B=2-368
3W1BX-ray2.4 ÅB=485-495
3W1GX-ray2.55 ÅB=485-495
7SGLEM3.0 ÅD=1-692
7TYREM3.33 ÅC=1-692

More AlphaFold highlights

About this viewer

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