2R9V

Crystal structure of ATP synthase subunit alpha (TM1612) from Thermotoga maritima at 2.10 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0005886	cellular_component	plasma membrane
A	0006754	biological_process	ATP biosynthetic process
A	0015986	biological_process	proton motive force-driven ATP synthesis
A	0032559	molecular_function	adenyl ribonucleotide binding
A	0043531	molecular_function	ADP binding
A	0045259	cellular_component	proton-transporting ATP synthase complex
A	0045261	cellular_component	proton-transporting ATP synthase complex, catalytic core F(1)
A	0046034	biological_process	ATP metabolic process
A	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
A	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
A	1902600	biological_process	proton transmembrane transport

Functional Information from PROSITE/UniProt

site_id	PS00152
Number of Residues	10
Details	ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS

Chain	Residue	Details
A	PRO356-SER365

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01346

Chain	Residue	Details
A	GLY170

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site_id	SWS_FT_FI2
Number of Residues	1
Details	SITE: Required for activity => ECO:0000255|HAMAP-Rule:MF_01346

Chain	Residue	Details
A	SER363

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
A	ARG366

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site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
A	GLN201
A	LYS202
A	LYS176

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