3AOU

Structure of the Na+ unbound rotor ring modified with N,N f-Dicyclohexylcarbodiimide of the Na+-transporting V-ATPase

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	ATP-synt_C	e3aouA1	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	ATP-synt_C	e3aouD1	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	ATP-synt_C	e3aouE1	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)
H	ATP-synt_C	e3aouH1	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)
J	ATP-synt_C	e3aouJ1	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	ATP-synt_C	e3aouB1	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	ATP-synt_C	e3aouC1	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)
F	ATP-synt_C	e3aouF1	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)
G	ATP-synt_C	e3aouG1	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)
I	ATP-synt_C	e3aouI1	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	1.20.120.610	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	lithium bound rotor ring of v- atpase	CATH (4.3.0)
D	1.20.120.610	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	lithium bound rotor ring of v- atpase	CATH (4.3.0)
E	1.20.120.610	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	lithium bound rotor ring of v- atpase	CATH (4.3.0)
H	1.20.120.610	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	lithium bound rotor ring of v- atpase	CATH (4.3.0)
J	1.20.120.610	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	lithium bound rotor ring of v- atpase	CATH (4.3.0)
B	1.20.120.610	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	lithium bound rotor ring of v- atpase	CATH (4.3.0)
C	1.20.120.610	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	lithium bound rotor ring of v- atpase	CATH (4.3.0)
F	1.20.120.610	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	lithium bound rotor ring of v- atpase	CATH (4.3.0)
G	1.20.120.610	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	lithium bound rotor ring of v- atpase	CATH (4.3.0)
I	1.20.120.610	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	lithium bound rotor ring of v- atpase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	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, B, C, D, E A, B, C, D, E, F, G, H, I, J	V-type sodium ATPase subunit K	monoatomic cation transmembrane transporter activity proton transmembrane transporter activity primary active transmembrane transporter activity ATPase-coupled transmembrane transporter activity proton-transporting ATPase activity, rotational mechanism ATPase-coupled monoatomic cation transmembrane transporter activity ATP-dependent activity active monoatomic ion transmembrane transporter activity ATPase-coupled ion transmembrane transporter activity active transmembrane transporter activity ATPase activity, coupled to transmembrane movement of ions, rotational mechanism inorganic molecular entity transmembrane transporter activity inorganic cation transmembrane transporter activity monoatomic ion transmembrane transporter activity transporter activity monoatomic cation transmembrane transporter activity proton transmembrane transporter activity primary active transmembrane transporter activity ATPase-coupled transmembrane transporter activity proton-transporting ATPase activity, rotational mechanism ATPase-coupled monoatomic cation transmembrane transporter activity ATP-dependent activity active monoatomic ion transmembrane transporter activity ATPase-coupled ion transmembrane transporter activity active transmembrane transporter activity ATPase activity, coupled to transmembrane movement of ions, rotational mechanism 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 binding	localization transport monoatomic ion transport monoatomic cation transport establishment of localization sodium ion transport metal ion transport	ATPase dependent transmembrane transport complex protein-containing complex ATPase complex catalytic complex membrane membrane protein complex proton-transporting V-type ATPase complex transporter complex proton-transporting two-sector ATPase complex, proton-transporting domain cation-transporting ATPase complex cellular anatomical structure proton-transporting two-sector ATPase complex transmembrane transporter complex proton-transporting V-type ATPase, V0 domain ATPase dependent transmembrane transport complex protein-containing complex ATPase complex catalytic complex membrane membrane protein complex proton-transporting V-type ATPase complex transporter complex proton-transporting two-sector ATPase complex, proton-transporting domain cation-transporting ATPase complex cellular anatomical structure proton-transporting two-sector ATPase complex transmembrane transporter complex proton-transporting V-type ATPase, V0 domain cell periphery plasma membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR035921	F/V-ATP synthase subunit C superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR000245	V-ATPase proteolipid subunit	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR002379	V-ATPase proteolipid subunit C-like domain	Domain

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	PDBTM	Annotated as membrane protein by PDBTM

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Chains	External Link	Comment
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	MemProtMD	Annotated as membrane protein by MemProtMD

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.