P53041: Serine/threonine-protein phosphatase 5 (PPP5C)

Serine/threonine-protein phosphatase 5 (PPP5C) is a 499-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P53041.

Gene
PPP5C
Organism
Homo sapiens
Length
499 residues
Mean pLDDT
92.8
Model
AF-P53041-F1 v6
Model created
1 Aug 2025
PDB structures
22

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Model confidence (pLDDT)

The mean pLDDT of this model is 92.8 (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 right10%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

Serine/threonine-protein phosphatase that dephosphorylates a myriad of proteins involved in different signaling pathways including the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT (PubMed:14734805, PubMed:14764652, PubMed:14871926, PubMed:15383005, PubMed:15546861, PubMed:16260606, PubMed:16790549, PubMed:16892053, PubMed:19176521, PubMed:19948726, PubMed:21144835, PubMed:22399290, PubMed:22781750, PubMed:23102700, PubMed:30699359, PubMed:9000529). Implicated in wide ranging cellular processes, including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian…

Subunit structure

Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (PubMed:29127155). Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-chaperones STIP1/HOP and PTGES3/p23…

Subcellular location

Nucleus, Cytoplasm, Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4ZX2X-ray1.23 ÅA=169-499
3H63X-ray1.3 ÅA/C=176-490
3H62X-ray1.4 ÅB/C=176-490
3H61X-ray1.45 ÅA/D=176-490
3H68X-ray1.5 ÅA/D=176-490
1S95X-ray1.6 ÅA/B=169-499
3H67X-ray1.65 ÅA/D=176-490
5WG8X-ray1.65 ÅA=169-499
3H64X-ray1.9 ÅA/D=176-490
5UI1X-ray1.96 ÅA/B/C/D=169-499
3H60X-ray2.0 ÅA/B=176-490
4ZVZX-ray2.0 ÅA/B/C/D=169-499
3H69X-ray2.1 ÅA/D=176-490
5HPEX-ray2.27 ÅA=175-499
1A17X-ray2.45 ÅA=16-181
3H66X-ray2.59 ÅA/B=176-490
1WAOX-ray2.9 Å1/2/3/4=23-499
8GAEEM3.3 ÅE=1-499
8GFTEM3.8 ÅE=1-499
7ZR5EM3.9 ÅP=17-499

Showing 20 of 22 experimental structures (best resolution first).

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