O75306: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial (NDUFS2)

NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial (NDUFS2) is a 463-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O75306.

Gene
NDUFS2
Organism
Homo sapiens
Length
463 residues
Mean pLDDT
89.1
Model
AF-O75306-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 89.1 (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 accurate81%
70 to 90Confident: backbone generally right11%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions7%

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:22036843, PubMed:28031252, PubMed:30922174). Essential for the catalytic activity of complex I (PubMed:22036843, PubMed:30922174). Essential for the assembly of complex I (By similarity). 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 (By similarity).…

Subunit structure

Core subunit of respiratory chain NADH dehydrogenase (Complex I) which is composed of 45 different subunits. Component of the iron-sulfur (IP) fragment of the enzyme (PubMed:12611891). Interacts with NDUFAF3 (PubMed:19463981). Interacts with NDUFAF7 (PubMed:20406883, PubMed:24089531). Interacts with CERS2 (By similarity)

Subcellular location

Mitochondrion inner membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9I4IEM2.63 ÅQ=1-463
9TI4EM2.66 ÅQ=34-463
5XTBEM3.4 ÅQ=79-463
9CWTEM3.44 ÅQ=1-463
5XTCEM3.7 ÅQ=34-79
5XTDEM3.7 ÅQ=34-463
5XTHEM3.9 ÅQ=34-463
5XTIEM17.4 ÅBQ/Q=34-463

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