Q86YN6: Peroxisome proliferator-activated receptor gamma coactivator 1-beta (PPARGC1B)

Peroxisome proliferator-activated receptor gamma coactivator 1-beta (PPARGC1B) is a 1023-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q86YN6.

Gene
PPARGC1B
Organism
Homo sapiens
Length
1023 residues
Mean pLDDT
50.1
Model
AF-Q86YN6-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 50.1 (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 accurate6%
70 to 90Confident: backbone generally right12%
50 to 70Low: treat with caution16%
Below 50Very low: often disordered regions67%

What pLDDT means and how to read it

Function

Plays a role of stimulator of transcription factors and nuclear receptors activities. Activates transcriptional activity of estrogen receptor alpha, nuclear respiratory factor 1 (NRF1) and glucocorticoid receptor in the presence of glucocorticoids. May play a role in constitutive non-adrenergic-mediated mitochondrial biogenesis as suggested by increased basal oxygen consumption and mitochondrial number when overexpressed. May be involved in fat oxidation and non-oxidative glucose metabolism and in the regulation of energy expenditure. Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner

Subunit structure

Interacts with hepatocyte nuclear factor 4-alpha/HNF4A, Sterol regulatory binding transcription factor 1/SREBF1, PPAR-alpha/PPARA, thyroid hormone receptor beta/THRB and host cell factor/HCFC1. Interacts with estrogen-related receptor gamma/ESRRG and alpha/ESRRA. Interacts with PRDM16 (By similarity). Interacts with estrogen receptor alpha/ESR1

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3SP6X-ray2.21 ÅB=153-163
6D0YX-ray2.68 ÅB=994-1023

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