P60712: Actin, cytoplasmic 1 (ACTB)

Actin, cytoplasmic 1 (ACTB) is a 375-residue protein from Bos taurus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P60712.

Gene
ACTB
Organism
Bos taurus
Length
375 residues
Mean pLDDT
95.4
Model
AF-P60712-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 95.4 (very high 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 accurate93%
70 to 90Confident: backbone generally right4%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells (By similarity). Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction (By similarity). In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA (By similarity). Plays a role in the assembly of the gamma-tubulin ring complex (gTuRC), which regulates the minus-end nucleation of alpha-beta tubulin heterodimers that grow into microtubule protafilaments (By…

Subunit structure

Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix (By similarity). Each actin can bind to 4 others (By similarity). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (By similarity). Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2,…

Subcellular location

Cytoplasm, cytoskeleton, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3UB5X-ray2.2 ÅA=2-375
3U4LX-ray2.4 ÅA=1-375
2BTFX-ray2.55 ÅA=2-375
2OANX-ray2.61 ÅA/B/C/D=1-375
1HLUX-ray2.65 ÅA=2-375
8OI6EM3.59 ÅA/B/C/D=1-375
9FJYEM3.79 ÅA/B/C/D=2-375
7PDZEM3.8 ÅI/J/K/L/N/O=1-375
9FJUEM3.84 ÅA/B/C/D=2-375
9FQREM5.0 ÅG6/Gz/Oi/Pj/Pl/Qp=1-375

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