Q91VD9: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial (Ndufs1)

NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial (Ndufs1) is a 727-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q91VD9.

Gene
Ndufs1
Organism
Mus musculus
Length
727 residues
Mean pLDDT
92.1
Model
AF-Q91VD9-F1 v6
Model created
1 Aug 2025
PDB structures
48

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Model confidence (pLDDT)

The mean pLDDT of this model is 92.1 (very high 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 accurate86%
70 to 90Confident: backbone generally right9%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions5%

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:27799543, PubMed:32072193, PubMed:38575788). Essential for catalysing the entry and efficient transfer of electrons within complex I (PubMed:27799543). Plays a key role in the assembly and stability of complex I and participates in the association of complex I with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes (PubMed:27799543)

Subunit structure

Core subunit of respiratory chain NADH dehydrogenase (Complex I) which is composed of 45 different subunits (PubMed:38575788). This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme (By similarity). Complex I associates with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes (PubMed:27799543). In astrocytes, less…

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 ÅG=1-727
8OLTEM2.84 ÅG=1-727
8RGREM2.9 Å3=1-727
6ZTQEM3.0 ÅG=1-727
8RGPEM3.0 Å3=1-727
8RGQEM3.0 Å3=1-727
7B93EM3.04 ÅG=1-727
6ZR2EM3.1 ÅG=1-727
8RGTEM3.1 Å3=1-727
8XNLEM3.1 ÅG=1-727
7AK5EM3.17 ÅG=1-715
8CA3EM3.2 ÅG=1-727
8IAPEM3.2 ÅG=1-727
8IBAEM3.2 ÅG=1-727
8IC3EM3.2 ÅG=1-727
8CA4EM3.25 ÅG=1-727
6G2JEM3.3 ÅG=1-727
8IB5EM3.3 ÅG=1-727
8IBEEM3.3 ÅG=1-727
8PW6EM3.3 Å3=1-727

Showing 20 of 48 experimental structures (best resolution first).

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