AlphaFold predicted structure
MT-ATP6 · P00846


Mean pLDDT
88.9/ 100
Confident
226 residues
Confidence breakdown
- Very high(≥ 90)55%
- Confident(70–90)44%
- Low(50–70)1%
- Very low(< 50)0%
AlphaFold (Jumper et al., 2021) · CC BY 4.0
mitochondrially encoded ATP synthase membrane subunit 6
Annotations refreshed 8 hours ago.
Diagnostic Grade (Green)
Ataxia and cerebellar anomalies - narrow panel
MITOCHONDRIALHereditary ataxia
MITOCHONDRIALHereditary ataxia with onset in adulthood
MITOCHONDRIALHereditary neuropathy
MITOCHONDRIALHereditary neuropathy or pain disorder
MITOCHONDRIALLikely inborn error of metabolism
MITOCHONDRIALMitochondrial disorders
MITOCHONDRIALNARP syndrome or maternally inherited Leigh syndrome
MITOCHONDRIAL+13 more panels — install the extension to see the full list inline on any page.
NARP syndrome
Leber hereditary optic neuropathy
Leigh syndrome
mitochondrial disease
mitochondrial complex 5 (ATP synthase) deficiency, mitochondrial type 1
MELAS syndrome
MERRF
MERRF syndrome
Isolated cytochrome C oxidase deficiency
leigh syndrome due to mitochondrial complex iv deficiency
Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.
ATP synthase F(0) complex subunit a
Subunit a, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that 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 (Probable). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed:37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed:37244256). 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 (Probable). With the subunit c (ATP5MC1), forms the proton-conducting channel in the F(0) domain, that contains two crucial half-channels (inlet and outlet) that facilitate proton movement from the mitochondrial intermembrane space (IMS) into the matrix (PubMed:37244256). Protons are taken up via the inlet half-channel and released through the outlet half-channel, following a Grotthuss mechanism (PubMed:37244256)
Curated MONDO disease pages that list MT-ATP6 among their top associated genes.
MT-ATP6 · P00846


Mean pLDDT
88.9/ 100
Confident
226 residues
Confidence breakdown
AlphaFold (Jumper et al., 2021) · CC BY 4.0