Q13451: Peptidyl-prolyl cis-trans isomerase FKBP5 (FKBP5)

Peptidyl-prolyl cis-trans isomerase FKBP5 (FKBP5) is a 457-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13451.

Gene
FKBP5
Organism
Homo sapiens
Length
457 residues
Mean pLDDT
92.5
Model
AF-Q13451-F1 v6
Model created
1 Aug 2025
PDB structures
138

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Model confidence (pLDDT)

The mean pLDDT of this model is 92.5 (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 accurate88%
70 to 90Confident: backbone generally right4%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions6%

What pLDDT means and how to read it

Function

Immunophilin protein with PPIase and co-chaperone activities (PubMed:11350175). Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded (PubMed:12538866). Acts as a regulator of Akt/AKT1 activity by promoting the interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1 (PubMed:28147277, PubMed:28363942). Interacts with IKBKE and IKBKB which facilitates IKK complex assembly leading to increased IKBKE and IKBKB kinase…

Subunit structure

Part of a heteromultimeric cytoplasmic complex with HSP90AA1, HSPA1A/HSPA1B and steroid receptors. Upon ligand binding dissociates from the complex and FKBP4 takes its place (By similarity). Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP (PubMed:7693698). Interacts with NR3C1 (By similarity). Interacts with Akt/AKT1 and PHLPP1;…

Subcellular location

Cytoplasm, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7AOTX-ray0.85 ÅA=16-140
7APWX-ray0.89 ÅA=16-140
8R5KX-ray0.89 ÅA=16-140
7APSX-ray0.94 ÅA/B=16-140
3O5QX-ray0.96 ÅA=16-140
6TX6X-ray0.98 ÅA=16-140
8CHNX-ray0.99 ÅA=16-140
3O5PX-ray1.0 ÅA=16-140
4DRQX-ray1.0 ÅA=16-140
5OBKX-ray1.0 ÅA=16-140
8CHPX-ray1.0 ÅA=16-140
8CHQX-ray1.01 ÅA=16-140
4JFMX-ray1.02 ÅA=16-140
4TX0X-ray1.03 ÅA=16-140
4JFIX-ray1.05 ÅA=16-139
6TX4X-ray1.06 ÅA=16-140
4DRNX-ray1.07 ÅA=16-140
4JFJX-ray1.08 ÅA=16-140
4W9QX-ray1.08 ÅA=16-140
6TX5X-ray1.08 ÅA=16-140

Showing 20 of 138 experimental structures (best resolution first).

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