Q9D0M3: Cytochrome c1, heme protein, mitochondrial (Cyc1)

Cytochrome c1, heme protein, mitochondrial (Cyc1) is a 325-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9D0M3.

Gene
Cyc1
Organism
Mus musculus
Length
325 residues
Mean pLDDT
84.8
Model
AF-Q9D0M3-F1 v6
Model created
1 Aug 2025
PDB structures
18

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.8 (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 accurate72%
70 to 90Confident: backbone generally right5%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions15%

What pLDDT means and how to read it

Function

Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol…

Subunit structure

Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 11 subunits (PubMed:34616041, PubMed:38575788). The complex is composed of 3 respiratory subunits cytochrome b, cytochrome c1 and Rieske protein UQCRFS1, 2 core protein subunits UQCRC1/QCR1 and UQCRC2/QCR2, and 6 low-molecular weight protein subunits UQCRH/QCR6,…

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
7O3HEM2.6 ÅD/O=85-325
7O37EM3.2 ÅD/O=85-325
7O3CEM3.3 ÅD/O=85-325
8PW6EM3.3 ÅD/O=1-325
8IAREM3.4 ÅAD/Ad=1-325
8IB7EM3.4 ÅAD/Ad=1-325
8PW7EM3.5 ÅD/O=1-325
7O3EEM3.6 ÅD/O=85-325
8IBCEM3.6 ÅAD/Ad=1-325
8PW5EM3.6 ÅD/O=1-325
8UCAEM3.7 Å3D/3O=85-325
8IBGEM3.8 ÅAD/Ad=1-325
8IC5EM4.1 ÅAD/Ad=1-325
8IAOEM4.2 ÅAD/Ad=1-325
8IBDEM4.2 ÅAD/Ad=1-325
8IB4EM4.3 ÅAD/Ad=1-325
8IB9EM4.3 ÅAD/Ad=1-325
8IC2EM6.3 ÅAD/Ad=1-325

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