O14646: Chromodomain-helicase-DNA-binding protein 1 (CHD1)

Chromodomain-helicase-DNA-binding protein 1 (CHD1) is a 1710-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O14646.

Gene
CHD1
Organism
Homo sapiens
Length
1710 residues
Mean pLDDT
62.1
Model
AF-O14646-F1 v6
Model created
1 Aug 2025
PDB structures
13

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Model confidence (pLDDT)

The mean pLDDT of this model is 62.1 (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 accurate9%
70 to 90Confident: backbone generally right42%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions40%

What pLDDT means and how to read it

Function

ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. Is also associated with histone deacetylase (HDAC) activity (By similarity). Required for the bridging of SNF2, the FACT complex, the PAF complex as well as the U2 snRNP…

Subunit structure

Component of the SAGA complex (By similarity). Interacts with BCLAF1, NCoR, SRP20 and SAFB (By similarity). Specifically interacts with methylated H3K4me2 and H3K4me3. Interacts with the FACT complex, the PAF complex and the U2 snRNP. Interacts directly with PAF1, SFA3A1, SFA3A2, SFA3A3, SNF2 and SSRP1

Subcellular location

Nucleus, Cytoplasm

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5AFWX-ray1.6 ÅA=270-443
4B4CX-ray1.62 ÅA=1119-1327
4O42X-ray1.87 ÅA=268-443
4NW2X-ray1.9 ÅA/C=268-443
2B2YX-ray2.35 ÅA/B=268-443, C=268-373
2B2WX-ray2.4 ÅA/B=268-443, C=268-373
2B2TX-ray2.45 ÅA/B=268-443, C=268-373
2B2VX-ray2.65 ÅA/B=268-443, C=268-373
2B2UX-ray2.95 ÅA/B=268-443, C=268-373
8UMGX-ray3.1 ÅA/B/C=268-445
9EAREM3.1 ÅW=2-1327
9NH8EM3.2 ÅW=2-1327
2N39NMRA=1409-1511

More AlphaFold highlights

About this viewer

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