Q02790: Peptidyl-prolyl cis-trans isomerase FKBP4 (FKBP4)

Peptidyl-prolyl cis-trans isomerase FKBP4 (FKBP4) is a 459-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q02790.

Gene
FKBP4
Organism
Homo sapiens
Length
459 residues
Mean pLDDT
90.4
Model
AF-Q02790-F1 v6
Model created
1 Aug 2025
PDB structures
12

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Model confidence (pLDDT)

The mean pLDDT of this model is 90.4 (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 right5%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions9%

What pLDDT means and how to read it

Function

Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Also acts as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria

Subunit structure

Homodimer (By similarity). Interacts with GLMN (PubMed:12604780). Associates with HSP90AA1 and HSP70 in steroid hormone receptor complexes. Also interacts with peroxisomal phytanoyl-CoA alpha-hydroxylase (PHYH). Interacts with NR3C1 and dynein. Interacts with HSF1 in the HSP90 complex. Associates with tubulin. Interacts with MAPT/TAU (By similarity). Interacts (via TPR domain) with S100A1,…

Subcellular location

Cytoplasm, cytosol, Mitochondrion, Nucleus, Cytoplasm, cytoskeleton, Cell projection, axon

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4LAYX-ray1.7 ÅA=1-260
4DRJX-ray1.8 ÅA=1-140
4LAVX-ray1.8 ÅA/B=16-260
1Q1CX-ray1.9 ÅA=2-260
4LAXX-ray2.01 ÅA=16-260
6RCYX-ray2.3 ÅA=1-148
1N1AX-ray2.4 ÅA/B=1-140
4LAWX-ray2.4 ÅA/B=16-260
1P5QX-ray2.8 ÅA/B/C=146-459
1QZ2X-ray3.0 ÅA/B/C=145-459
4TW8X-ray3.0 ÅA/B=21-255
8FFVEM3.01 ÅD=1-459

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