Q6P4F2: Ferredoxin-2, mitochondrial (FDX2)

Ferredoxin-2, mitochondrial (FDX2) is a 183-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q6P4F2.

Gene
FDX2
Organism
Homo sapiens
Length
183 residues
Mean pLDDT
76.6
Model
AF-Q6P4F2-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 76.6 (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 accurate51%
70 to 90Confident: backbone generally right8%
50 to 70Low: treat with caution27%
Below 50Very low: often disordered regions14%

What pLDDT means and how to read it

Function

Electron donor, of the core iron-sulfur cluster (ISC) assembly complex, that acts to reduce the persulfide into sulfide during [2Fe-2S] clusters assembly on the scaffolding protein ISCU (PubMed:28001042). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis (By similarity). This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner (By similarity). Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the…

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). Form a heterodimer complex with NFS1 (PubMed:29097656). Interacts (in both their reduced and oxidized states) with the cysteine desulfurase complex; this interaction stimulates cysteine…

Subcellular location

Mitochondrion, Mitochondrion matrix

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2Y5CX-ray1.7 ÅA/B=66-171
8RMCEM2.26 ÅI=66-183
8RMFEM2.33 ÅI=65-183
8RMGEM2.46 ÅI=65-183
8RMDEM2.52 ÅI=66-183

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