3U2F

ATP synthase c10 ring in proton-unlocked conformation at PH 8.3

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: PDBTM
Membrane Protein Annotation: MemProtMD
Membrane Protein Annotation: mpstruc
Protein Modification Annotation

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth K]	ATP-synt_C	e3u2fK1	A: extended segments	X: F1F0 ATP synthase subunit C (From Topology)	H: F1F0 ATP synthase subunit C (From Topology)	T: F1F0 ATP synthase subunit C	F: ATP-synt_C	ECOD (1.6)
B [auth L]	ATP-synt_C	e3u2fL1	A: extended segments	X: F1F0 ATP synthase subunit C (From Topology)	H: F1F0 ATP synthase subunit C (From Topology)	T: F1F0 ATP synthase subunit C	F: ATP-synt_C	ECOD (1.6)
D [auth N]	ATP-synt_C	e3u2fN1	A: extended segments	X: F1F0 ATP synthase subunit C (From Topology)	H: F1F0 ATP synthase subunit C (From Topology)	T: F1F0 ATP synthase subunit C	F: ATP-synt_C	ECOD (1.6)
C [auth M]	ATP-synt_C	e3u2fM1	A: extended segments	X: F1F0 ATP synthase subunit C (From Topology)	H: F1F0 ATP synthase subunit C (From Topology)	T: F1F0 ATP synthase subunit C	F: ATP-synt_C	ECOD (1.6)
E [auth O]	ATP-synt_C	e3u2fO1	A: extended segments	X: F1F0 ATP synthase subunit C (From Topology)	H: F1F0 ATP synthase subunit C (From Topology)	T: F1F0 ATP synthase subunit C	F: ATP-synt_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth K]	1.20.20.10	Mainly Alpha	Up-down Bundle	F1FO ATP Synthase	F1F0 ATP synthase subunit C	CATH (4.3.0)
B [auth L]	1.20.20.10	Mainly Alpha	Up-down Bundle	F1FO ATP Synthase	F1F0 ATP synthase subunit C	CATH (4.3.0)
D [auth N]	1.20.20.10	Mainly Alpha	Up-down Bundle	F1FO ATP Synthase	F1F0 ATP synthase subunit C	CATH (4.3.0)
C [auth M]	1.20.20.10	Mainly Alpha	Up-down Bundle	F1FO ATP Synthase	F1F0 ATP synthase subunit C	CATH (4.3.0)
E [auth O]	1.20.20.10	Mainly Alpha	Up-down Bundle	F1FO ATP Synthase	F1F0 ATP synthase subunit C	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth K], B [auth L], C [auth M], D [auth N], E [auth O]	PF00137	ATP synthase subunit C (ATP-synt_C)	ATP synthase subunit C	This domain is found in the subunit c of ATP synthases and similar sequences from all cellular organisms. It forms two alpha-helices [1-4].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth K], B [auth L], C [auth M], D [auth N], E [auth O]	ATP synthase subunit C, mitochondrial	binding lipid binding monoatomic cation transmembrane transporter activity proton transmembrane transporter activity inorganic molecular entity transmembrane transporter activity inorganic cation transmembrane transporter activity monoatomic ion transmembrane transporter activity transporter activity transmembrane transporter activity identical protein binding protein binding	ribose phosphate metabolic process ATP metabolic process ATP biosynthetic process nucleotide biosynthetic process carbohydrate derivative metabolic process purine ribonucleotide biosynthetic process purine ribonucleoside triphosphate biosynthetic process proton motive force-driven ATP synthesis nucleobase-containing compound metabolic process ribonucleotide biosynthetic process purine nucleotide metabolic process ribonucleotide metabolic process purine nucleoside triphosphate biosynthetic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process ribose phosphate metabolic process ATP metabolic process ATP biosynthetic process nucleotide biosynthetic process carbohydrate derivative metabolic process purine ribonucleotide biosynthetic process purine ribonucleoside triphosphate biosynthetic process proton motive force-driven ATP synthesis nucleobase-containing compound metabolic process ribonucleotide biosynthetic process purine nucleotide metabolic process ribonucleotide metabolic process purine nucleoside triphosphate biosynthetic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process purine ribonucleoside triphosphate metabolic process phosphate-containing compound metabolic process small molecule metabolic process phosphorus metabolic process ribose phosphate biosynthetic process ribonucleoside triphosphate metabolic process nucleoside phosphate metabolic process carbohydrate derivative biosynthetic process purine nucleoside triphosphate metabolic process nucleoside triphosphate biosynthetic process primary metabolic process nucleotide metabolic process nucleobase-containing compound biosynthetic process ribonucleoside triphosphate biosynthetic process purine-containing compound metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process nucleoside phosphate biosynthetic process metabolic process cellular process nucleoside triphosphate metabolic process purine ribonucleotide metabolic process purine nucleotide biosynthetic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle mitochondrial membrane organelle inner membrane membrane mitochondrial inner membrane organelle envelope mitochondrial envelope membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle mitochondrial membrane organelle inner membrane membrane mitochondrial inner membrane organelle envelope mitochondrial envelope organelle membrane cytosol mitochondrial intermembrane space membrane-enclosed lumen intracellular organelle lumen organelle envelope lumen organelle lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth K], B [auth L], C [auth M], D [auth N], E [auth O]	IPR035921	F/V-ATP synthase subunit C superfamily	Homologous Superfamily
A [auth K], B [auth L], C [auth M], D [auth N], E [auth O]	IPR038662	F1F0 ATP synthase subunit C superfamily	Homologous Superfamily
A [auth K], B [auth L], C [auth M], D [auth N], E [auth O]	IPR002379	V-ATPase proteolipid subunit C-like domain	Domain
A [auth K], B [auth L], C [auth M], D [auth N], E [auth O]	IPR020537	ATP synthase, F0 complex, subunit C, DCCD-binding site	Binding Site
A [auth K], B [auth L], C [auth M], D [auth N], E [auth O]	IPR000454	ATP synthase, F0 complex, subunit C	Family

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A [auth K], B [auth L], C [auth M], D [auth N], E [auth O]	PDBTM	Annotated as membrane protein by PDBTM

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Chains	External Link	Comment
A [auth K], B [auth L], C [auth M], D [auth N], E [auth O]	MemProtMD	Annotated as membrane protein by MemProtMD

Membrane Protein Annotation: mpstruc mpstruc Database Homepage

Chains	Resource Link	Group	Subgroup	Protein
A [auth K], B [auth L], C [auth M], D [auth N], E [auth O]	mpstruc	TRANSMEMBRANE PROTEINS: ALPHA-HELICAL	F-type ATPase	ATP synthase (F₁c₁₀), pH 8.3

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A [auth K], B [auth L], C [auth M], D [auth N], E [auth O]	FME	Parent Component: MET RESID: AA0021 , AA0566 PSI-MOD : N-formyl-L-methionine residue MOD:00030 , N-formyl-L-methionine (Met) MOD:00482 , N-[(L-histidin-1'-yl)methyl]-L-methionine (fMet) MOD:01890 , N-[(L-histidin-1'-yl)methyl]-L-methionine (Met) MOD:01891

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.