4Q4L

Crystal structure of an ATP synthase subunit beta 1 (F1-B1) from Burkholderia thailandensis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0005886	cellular_component	plasma membrane
A	0006754	biological_process	ATP biosynthetic process
A	0006811	biological_process	monoatomic ion transport
A	0015986	biological_process	proton motive force-driven ATP synthesis
A	0016020	cellular_component	membrane
A	0016887	molecular_function	ATP hydrolysis activity
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 PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 501

Chain	Residue
A	GLU250
A	ASP453
A	HOH607
A	HOH628
A	HOH640
A	HOH661

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PRO349-SER358

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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_01347

Chain	Residue	Details
A	GLY166

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