P07926: ATP synthase F(0) complex subunit C2, mitochondrial (ATP5MC2)

ATP synthase F(0) complex subunit C2, mitochondrial (ATP5MC2) is a 143-residue protein from Bos taurus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P07926.

Gene
ATP5MC2
Organism
Bos taurus
Length
143 residues
Mean pLDDT
72.4
Model
AF-P07926-F1 v6
Model created
1 Aug 2025
PDB structures
17

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Model confidence (pLDDT)

The mean pLDDT of this model is 72.4 (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 accurate50%
70 to 90Confident: backbone generally right4%
50 to 70Low: treat with caution18%
Below 50Very low: often disordered regions29%

What pLDDT means and how to read it

Function

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex…

Subunit structure

F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Interacts with DNAJC30; interaction is direct

Subcellular location

Mitochondrion membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6Z1REM3.29 ÅK/L/M/N/O/P/Q/R=69-143
6ZQMEM3.29 ÅK/L/M/N/O/P/Q/R=69-143
6Z1UEM3.47 ÅK/L/M/N/O/P/Q/R=69-143
6ZG7EM3.49 ÅK/L/M/N/O/P/Q/R=69-143
6ZG8EM3.49 ÅK/L/M/N/O/P/Q/R=69-143
6ZITEM3.49 ÅK/L/R=69-143
6ZIKEM3.66 ÅK/L/M/N/O/P/Q/R=69-143
6ZQNEM4.0 ÅK/L/M/N/O/P/Q/R=69-143
7AJFEM8.45 ÅAK/AL/AM/AN/AO/AP/AQ/AR/K/L/M/N/O/P/Q/R=69-143
7AJDEM9.0 ÅAK/AL/AM/AN/AO/AP/AQ/AR/K/L/M/N/O/P/Q/R=69-143
7AJBEM9.2 ÅAK/AL/AM/AN/AO/AP/AQ/AR/K/L/M/N/O/P/Q/R=69-143
7AJEEM9.4 ÅAK/AL/AM/AN/AO/AP/AQ/AR/K/L/M/N/O/P/Q/R=69-143
7AJHEM9.7 ÅAK/AL/AM/AN/AO/AP/AQ/AR/K/L/M/N/O/P/Q/R=69-143
7AJGEM10.7 ÅAK/AL/AM/AN/AO/AP/AQ/AR/K/L/M/N/O/P/Q/R=69-143
7AJIEM11.4 ÅAK/AL/AM/AN/AO/AP/AQ/AR/K/L/M/N/O/P/Q/R=69-143
7AJCEM11.9 ÅAK/AL/AM/AN/AO/AP/AQ/AR/K/L/M/N/O/P/Q/R=69-143
7AJJEM13.1 ÅAK/AL/AM/AN/AO/AP/AQ/AR/K/L/M/N/O/P/Q/R=69-143

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