P36887: cAMP-dependent protein kinase catalytic subunit alpha (PRKACA)

cAMP-dependent protein kinase catalytic subunit alpha (PRKACA) is a 351-residue protein from Sus scrofa. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P36887.

Gene
PRKACA
Organism
Sus scrofa
Length
351 residues
Mean pLDDT
95.6
Model
AF-P36887-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 95.6 (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 accurate94%
70 to 90Confident: backbone generally right3%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Phosphorylates a large number of substrates in the cytoplasm and the nucleus. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, histone H1.4 (H1-4), PSMC5/RPT6, PJA2, RYR2, RORA, SLC6A6, SOX9, UHRF1 and VASP. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts (By similarity). Involved in chondrogenesis by mediating phosphorylation of SOX9 (By similarity). Involved in the regulation of…

Subunit structure

A number of inactive tetrameric holoenzymes are produced by the combination of homo- or heterodimers of the different regulatory subunits associated with two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. The cAMP-dependent protein kinase catalytic subunit binds PJA2.…

Subcellular location

Cytoplasm, Cell membrane, Membrane, Nucleus, Mitochondrion

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1CDKX-ray2.0 ÅA/B=2-351
1CMKX-ray2.9 ÅE=2-351
1CTPX-ray2.9 ÅE=2-351

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