Q16595: Frataxin, mitochondrial (FXN)

Frataxin, mitochondrial (FXN) is a 210-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q16595.

Gene
FXN
Organism
Homo sapiens
Length
210 residues
Mean pLDDT
75.5
Model
AF-Q16595-F1 v6
Model created
1 Aug 2025
PDB structures
19

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Model confidence (pLDDT)

The mean pLDDT of this model is 75.5 (confident 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 accurate52%
70 to 90Confident: backbone generally right5%
50 to 70Low: treat with caution25%
Below 50Very low: often disordered regions18%

What pLDDT means and how to read it

Function

Functions as an activator of persulfide transfer to the scaffoding protein ISCU as component of the core iron-sulfur cluster (ISC) assembly complex and participates to the [2Fe-2S] cluster assembly (PubMed:12785837, PubMed:24971490). Accelerates sulfur transfer from NFS1 persulfide intermediate to ISCU and to small thiols such as L-cysteine and glutathione leading to persulfuration of these thiols and ultimately sulfide release (PubMed:24971490). Binds ferrous ion and is released from FXN upon the addition of both L-cysteine and reduced FDX2 during [2Fe-2S] cluster assembly (PubMed:29576242). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a…

Subunit structure

Component of the mitochondrial core iron-sulfur cluster (ISC) complex composed of NFS1, LYRM4, NDUFAB1, ISCU, FXN, and FDX2; this complex is a heterohexamer containing two copies of each monomer (Probable). Homodimer (PubMed:31101807). Monomer (probable predominant form). Oligomer. Monomers and polymeric aggregates of >1 MDa have been isolated from mitochondria. A small fraction of heterologous…

Subcellular location

Mitochondrion, Cytoplasm, cytosol

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3T3LX-ray1.15 ÅA=82-210
3T3KX-ray1.24 ÅA=82-210
3S4MX-ray1.3 ÅA=82-210
3S5EX-ray1.31 ÅA=82-210
3T3TX-ray1.38 ÅA/B/C/D=82-210
3S5DX-ray1.5 ÅA=82-210
3S5FX-ray1.5 ÅA/B=82-210
9HO5X-ray1.5 ÅA=90-210
3T3XX-ray1.57 ÅA/B=82-210
3T3JX-ray1.7 ÅA=82-210
9HO4X-ray1.76 ÅA=93-206
1EKGX-ray1.8 ÅA=84-210
9HO6X-ray2.0 ÅA/B=90-210
8PK8EM2.49 ÅE=81-210
8RMEEM2.49 ÅI=81-210
8PK9EM2.58 ÅE=81-210
6NZUEM3.2 ÅI/J=81-210
5KZ5EM14.3 ÅA/B/C/D/E/F/G/H/I/J/K/L=42-210
1LY7NMRA=90-210

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