Q12824: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin… (SMARCB1)

SWI/SNF-related matrix-associated actin-dependent regulator of chromatin… (SMARCB1) is a 385-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q12824.

Gene
SMARCB1
Organism
Homo sapiens
Length
385 residues
Mean pLDDT
80.8
Model
AF-Q12824-F1 v6
Model created
1 Aug 2025
PDB structures
17

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Model confidence (pLDDT)

The mean pLDDT of this model is 80.8 (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 accurate52%
70 to 90Confident: backbone generally right26%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions11%

What pLDDT means and how to read it

Function

Core component of the BAF (hSWI/SNF) complex. This ATP-dependent chromatin-remodeling complex plays important roles in cell proliferation and differentiation, in cellular antiviral activities and inhibition of tumor formation. The BAF complex is able to create a stable, altered form of chromatin that constrains fewer negative supercoils than normal. This change in supercoiling would be due to the conversion of up to one-half of the nucleosomes on polynucleosomal arrays into asymmetric structures, termed altosomes, each composed of 2 histones octamers. Stimulates in vitro the remodeling activity of SMARCA4/BRG1/BAF190A. Involved in activation of CSF1 promoter. Belongs to the neural…

Subunit structure

Component of the multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The canonical complex contains a catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes may also be present…

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
5GJKX-ray2.05 ÅB=183-249
5L7AX-ray2.1 ÅA/B/C/D=184-252
6KZ7X-ray2.28 ÅB/D=171-252
6KAGX-ray2.6 ÅA=169-385
6LTHEM3.0 ÅM=1-385
7VDVEM3.4 ÅV=1-385
9RL4EM3.5 ÅM=1-385
6LTJEM3.7 ÅM=1-113, M=172-385
9RN2EM4.1 ÅM=1-385
9RMCEM4.2 ÅM=1-385
7Y8REM4.4 ÅM=1-385
9RN1EM5.9 ÅM=1-385
5AJ1NMRA=2-113
5L7BNMRA=184-258
6AX5NMRA=183-265
6LZPNMRA=171-258
6UCHNMRA=351-385

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