P01096: ATPase inhibitor, mitochondrial (ATP5IF1)

ATPase inhibitor, mitochondrial (ATP5IF1) is a 109-residue protein from Bos taurus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P01096.

Gene
ATP5IF1
Organism
Bos taurus
Length
109 residues
Mean pLDDT
78.1
Model
AF-P01096-F1 v6
Model created
1 Aug 2025
PDB structures
27

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Model confidence (pLDDT)

The mean pLDDT of this model is 78.1 (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 accurate48%
70 to 90Confident: backbone generally right18%
50 to 70Low: treat with caution19%
Below 50Very low: often disordered regions15%

What pLDDT means and how to read it

Function

Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase (PubMed:10831597, PubMed:12923572, PubMed:17895376, PubMed:18687699, PubMed:21192948, PubMed:7397110). Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme…

Subunit structure

Homodimer; represents the active form and is present at a pH value below 6.5. Homotetramer; represents the inactive form and is present at a pH value above 7.0

Subcellular location

Mitochondrion

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2V7QX-ray2.1 ÅJ=26-85
1GMJX-ray2.2 ÅA/B/C/D=26-109
1OHHX-ray2.8 ÅH=26-109
4TSFX-ray3.2 ÅH/I=26-85
4TT3X-ray3.21 ÅH/I/J=26-85
6YY0EM3.23 ÅJ=26-85
6Z1REM3.29 ÅJ=26-85
6ZQMEM3.29 ÅJ=26-85
4Z1MX-ray3.3 ÅH/I/J=26-85
9W2REM3.4 ÅJ=26-85
6Z1UEM3.47 ÅJ=26-85
6ZPOEM4.0 ÅJ=26-85
6ZQNEM4.0 ÅJ=26-85
9W2SEM4.0 ÅJ=26-85
5LQZEM7.0 ÅJ=26-85
5LQYEM7.8 ÅJ=26-85
5LQXEM7.9 ÅJ=26-85
7AJFEM8.45 ÅAJ/J=26-109
7AJDEM9.0 ÅAJ/J=26-85
7AJBEM9.2 ÅAJ/J=26-85

Showing 20 of 27 experimental structures (best resolution first).

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