P07143: Cytochrome c1, heme protein, mitochondrial (CYT1)

Cytochrome c1, heme protein, mitochondrial (CYT1) is a 309-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P07143.

Gene
CYT1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
309 residues
Mean pLDDT
87.8
Model
AF-P07143-F1 v6
Model created
1 Aug 2025
PDB structures
23

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Model confidence (pLDDT)

The mean pLDDT of this model is 87.8 (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 accurate77%
70 to 90Confident: backbone generally right6%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions9%

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 10 subunits. The complex is composed of 3 respiratory subunits cytochrome b (COB), cytochrome c1 (CYT1) and Rieske protein (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10…

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
3CX5X-ray1.9 ÅD/O=62-309
1EZVX-ray2.3 ÅD=62-306
1KB9X-ray2.3 ÅD=62-307
2IBZX-ray2.3 ÅD=62-309
8YIOEM2.35 ÅD/O=62-309
9ETZEM2.4 ÅD/O=62-308
8YHQEM2.42 ÅD/M=62-309
1P84X-ray2.5 ÅD=62-307
3CXHX-ray2.5 ÅD/O=62-309
8ZJCEM2.5 ÅD/O=62-309
8ZMTEM2.52 ÅD/O=62-309
9BPBEM2.57 ÅD/N=1-309
8YILEM2.58 ÅD/O=62-309
8YINEM2.74 ÅD/O=62-309
6T0BEM2.8 ÅD/O=62-309
1KYOX-ray2.97 ÅD/O=62-309
4PD4X-ray3.04 ÅD=62-309
6YMXEM3.17 ÅD/O=62-309
8E7SEM3.2 ÅL/l=1-309
6GIQEM3.23 ÅD/O=1-309

Showing 20 of 23 experimental structures (best resolution first).

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