Q91WD5: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial (Ndufs2)

NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial (Ndufs2) is a 463-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q91WD5.

Gene
Ndufs2
Organism
Mus musculus
Length
463 residues
Mean pLDDT
89.0
Model
AF-Q91WD5-F1 v6
Model created
1 Aug 2025
PDB structures
52

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Model confidence (pLDDT)

The mean pLDDT of this model is 89.0 (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 accurate80%
70 to 90Confident: backbone generally right12%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions6%

What pLDDT means and how to read it

Function

Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:26437605, PubMed:29887397, PubMed:31297047, PubMed:38575788). Essential for the catalytic activity and assembly of complex I (PubMed:26437605, PubMed:29887397, PubMed:31297047). Redox-sensitive, critical component of the oxygen-sensing pathway in the pulmonary vasculature which plays a key role in acute pulmonary oxygen-sensing and hypoxic pulmonary vasoconstriction (PubMed:30922174). Plays an important role in carotid body sensing of hypoxia (PubMed:26437605, PubMed:29887397).…

Subunit structure

Core subunit of respiratory chain NADH dehydrogenase (Complex I) which is composed of 45 different subunits (PubMed:38575788). Component of the iron-sulfur (IP) fragment of the enzyme. Interacts with NDUFAF3. Interacts with NDUFAF7 (By similarity). Interacts with CERS2 (PubMed:32279995)

Subcellular location

Mitochondrion inner membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8OM1EM2.39 ÅD=1-463
8OLTEM2.84 ÅD=1-463
8RGREM2.9 ÅD=1-463
6ZTQEM3.0 ÅD=1-463
8RGPEM3.0 ÅD=1-463
8RGQEM3.0 ÅD=1-463
7B93EM3.04 ÅD=1-463
6ZR2EM3.1 ÅD=1-463
8RGTEM3.1 ÅD=1-463
8XNLEM3.1 ÅD=1-463
7AK5EM3.17 ÅD=1-463
8CA3EM3.2 ÅD=1-463
8IAPEM3.2 ÅD=1-463
8IBAEM3.2 ÅD=1-463
8IC3EM3.2 ÅD=1-463
8IC4EM3.2 ÅD=1-463
6G2JEM3.3 ÅD=1-463
8IB5EM3.3 ÅD=1-463
8IB6EM3.3 ÅD=1-463
8IBBEM3.3 ÅD=1-463

Showing 20 of 52 experimental structures (best resolution first).

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