Q9UKL0: REST corepressor 1 (RCOR1)

REST corepressor 1 (RCOR1) is a 485-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UKL0.

Gene
RCOR1
Organism
Homo sapiens
Length
485 residues
Mean pLDDT
68.5
Model
AF-Q9UKL0-F1 v6
Model created
1 Aug 2025
PDB structures
102

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Model confidence (pLDDT)

The mean pLDDT of this model is 68.5 (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 accurate37%
70 to 90Confident: backbone generally right15%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions38%

What pLDDT means and how to read it

Function

Essential component of the BHC complex, a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. In the BHC complex, it serves as a molecular beacon for the recruitment of molecular machinery, including MeCP2 and SUV39H1, that imposes silencing across a chromosomal interval. Plays a central role in demethylation of Lys-4 of histone H3 by promoting demethylase activity of KDM1A on core histones and nucleosomal substrates. It also protects KDM1A from the proteasome. Component of a…

Subunit structure

Interacts directly with GFI1 and GFI1B in a RCOR/GFI/KDM1A/HDAC complex. Interacts with INMS1 (By similarity). Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Interacts with REST. Interacts with the SMARCE1/BAF57, suggesting that the BHC complex…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5H6QX-ray2.53 ÅB=311-443
2IW5X-ray2.57 ÅB=289-485
5H6RX-ray2.6 ÅB=311-443
5L3DX-ray2.6 ÅB=4-485
6TUYX-ray2.6 ÅB=1-485
8Q1GX-ray2.6 ÅB=308-485
6KGMX-ray2.62 ÅB=311-443
6KGNX-ray2.62 ÅB=311-443
7CDCX-ray2.64 ÅB=311-443
9DBPX-ray2.66 ÅB=312-442
7CDEX-ray2.68 ÅB=311-443
7CDFX-ray2.68 ÅB=311-443
5X60X-ray2.69 ÅB=311-443
6KGKX-ray2.7 ÅB=311-443
6KGLX-ray2.7 ÅB=311-443
7ZRYX-ray2.7 ÅB=308-485
2UXNX-ray2.72 ÅB=289-485
8FRVX-ray2.72 ÅB=308-443
2UXXX-ray2.74 ÅB=289-485
8BOPX-ray2.74 ÅB=308-443

Showing 20 of 102 experimental structures (best resolution first).

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