P26447: Protein S100-A4 (S100A4)

Protein S100-A4 (S100A4) is a 101-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P26447.

Gene
S100A4
Organism
Homo sapiens
Length
101 residues
Mean pLDDT
86.4
Model
AF-P26447-F1 v6
Model created
1 Aug 2025
PDB structures
17

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Model confidence (pLDDT)

The mean pLDDT of this model is 86.4 (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 accurate64%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions5%

What pLDDT means and how to read it

Function

Calcium-binding protein that plays a role in various cellular processes including motility, angiogenesis, cell differentiation, apoptosis, and autophagy (PubMed:16707441, PubMed:23752197, PubMed:30713770). Increases cell motility and invasiveness by interacting with non-muscle myosin heavy chain (NMMHC) IIA/MYH9 (PubMed:16707441). Mechanistically, promotes filament depolymerization and increases the amount of soluble myosin-IIA, resulting in the formation of stable protrusions facilitating chemotaxis (By similarity). Also modulates the pro-apoptotic function of TP53 by binding to its C-terminal transactivation domain within the nucleus and reducing its protein levels (PubMed:23752197).…

Subunit structure

Homodimer. Interacts with PPFIBP1 in a calcium-dependent mode (PubMed:11836260). Interacts with PGLYRP1; this complex acts as a chemoattractant that promotes lymphocyte movement (PubMed:26654597, PubMed:30713770). Interacts with MYH9; this interaction increases cell motility (PubMed:16707441). Interacts with Annexin 2/ANXA2 (PubMed:28669632). Interacts with TP53; this interaction promotes TP53…

Subcellular location

Secreted, Nucleus, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4CFQX-ray1.37 ÅA/B/C/D=1-88
4CFRX-ray1.4 ÅA/B=1-101
3C1VX-ray1.5 ÅA/B/C/D=1-101
4ETOX-ray1.54 ÅA/B=1-93
2Q91X-ray1.63 ÅA/B=1-101
7PSQX-ray1.91 ÅA/C/E/G=1-100
3ZWHX-ray1.94 ÅA/B=1-101
3CGAX-ray2.03 ÅA/B=1-101
5LPUX-ray2.1 ÅC/D=1-101
4HSZX-ray2.25 ÅA/B/C/D=1-93
3KO0X-ray2.3 ÅA/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-101
7PSPX-ray2.61 ÅA/B=1-100
3M0WX-ray2.8 ÅA/B/C/D/E/F/G/H/I/J=2-101
6T58X-ray3.1 ÅA/B=1-93
1M31NMRA/B=1-101
2LNKNMRA/B=1-101
2MRDNMRA/B=1-101

More AlphaFold highlights

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