Q00975: Voltage-dependent N-type calcium channel subunit alpha-1B (CACNA1B)

Voltage-dependent N-type calcium channel subunit alpha-1B (CACNA1B) is a 2339-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q00975.

Gene
CACNA1B
Organism
Homo sapiens
Length
2339 residues
Mean pLDDT
59.9
Model
AF-Q00975-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 59.9 (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 accurate7%
70 to 90Confident: backbone generally right40%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions41%

What pLDDT means and how to read it

Function

Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. This alpha-1B subunit gives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group. They are involved in pain signaling (PubMed:25296916). Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons. Mediates Ca(2+) release probability at hippocampal neuronal soma and synaptic terminals (By similarity)

Subunit structure

Multisubunit complex consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1 ratio. The channel activity is directed by the pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this subunit is sufficient to generate voltage-sensitive calcium channel activity. The auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge regulate the channel activity.…

Subcellular location

Membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7VFSEM2.8 ÅA=1-2339
7MIXEM3.0 ÅA=1-2339
7VFUEM3.0 ÅA=1-2339
7VFVEM3.0 ÅA=1-2339
7MIYEM3.1 ÅA=1-2339
7VFWEM3.3 ÅA=1-2339
2LCMNMRA=1242-1269

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