Q56222: NADH-quinone oxidoreductase subunit 1 (nqo1)

NADH-quinone oxidoreductase subunit 1 (nqo1) is a 438-residue protein from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q56222.

Gene
nqo1
Organism
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Length
438 residues
Mean pLDDT
94.3
Model
AF-Q56222-F1 v6
Model created
1 Aug 2025
PDB structures
17

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Model confidence (pLDDT)

The mean pLDDT of this model is 94.3 (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 accurate92%
70 to 90Confident: backbone generally right4%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP. The Nqo1 subunit contains the NADH-binding site and the primary electron acceptor FMN

Subunit structure

NDH-1 is composed of 15 different subunits, Nqo1 to Nqo15. The complex has a L-shaped structure, with the hydrophobic arm (subunits Nqo7, Nqo8 and Nqo10 to Nqo14) embedded in the membrane and the hydrophilic peripheral arm (subunits Nqo1 to Nqo6, Nqo9 and Nqo15) protruding into the bacterial cytoplasm. The hydrophilic domain contains all the redox centers

Subcellular location

Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3I9VX-ray3.1 Å1/A=1-438
3IAMX-ray3.1 Å1/A=1-438
6Y11X-ray3.11 Å1/B=1-438
3IASX-ray3.15 Å1/A/J/S=1-438
6I1PX-ray3.21 Å1/B=1-438
2FUGX-ray3.3 Å1/A/J/S=1-438
4HEAX-ray3.3 Å1/B=1-438
6Q8WX-ray3.4 Å1/B=1-438
6Q8XX-ray3.51 Å1/B=1-438
6I0DX-ray3.6 Å1/B=1-438
6Q8OX-ray3.6 Å1/B=1-438
6ZIYEM4.25 Å1=1-438
6ZJLEM4.3 Å1=1-438
3M9SX-ray4.5 Å1/A=1-438
6ZJYEM5.5 Å1=1-438
6ZJNEM6.1 Å1=1-438
2YBBEM19.0 Å1=1-438

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