P04631: Protein S100-B (S100b)

Protein S100-B (S100b) is a 92-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P04631.

Gene
S100b
Organism
Rattus norvegicus
Length
92 residues
Mean pLDDT
92.7
Model
AF-P04631-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 92.7 (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 accurate84%
70 to 90Confident: backbone generally right12%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

Small zinc- and- and calcium-binding protein that is highly expressed in astrocytes and constitutes one of the most abundant soluble proteins in brain (PubMed:14621986, PubMed:15823027, PubMed:18949447, PubMed:20351179). Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer (PubMed:15823027). Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites (By similarity). Acts as a neurotrophic factor that promotes astrocytosis and axonal proliferation (By similarity). Involved in innervation of thermogenic adipose tissue by…

Subunit structure

Dimer of either two alpha chains, or two beta chains, or one alpha and one beta chain (By similarity). The S100B dimer binds two molecules of STK38 (By similarity). Interacts with CACYBP in a calcium-dependent manner (PubMed:12042313). Interacts with ATAD3A; this interaction probably occurs in the cytosol prior to ATAD3A mitochondrial targeting (PubMed:20351179). Interacts with S100A6 (By…

Subcellular location

Cytoplasm, Nucleus, Secreted

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1B4CNMRA/B=1-92
1DT7NMRA/B=1-92
1MWNNMRA/B=1-92
1QLKNMRA/B=1-92
1SYMNMRA/B=1-92
1XYDNMRA/B=1-92
2K7ONMRA/B=2-92

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