3QG1

Crystal structure of P-loop G239A mutant of subunit A of the A1AO ATP synthase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0015986	biological_process	proton motive force-driven ATP synthesis
A	0033178	cellular_component	proton-transporting two-sector ATPase complex, catalytic domain
A	0046034	biological_process	ATP metabolic process
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	1
Details	BINDING SITE FOR RESIDUE ACY A 589

Chain	Residue
A	PRO551

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MPD A 590

Chain	Residue
A	ASP420
A	LEU421
A	ASN431
A	TRP432
A	LEU433
A	HOH604

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site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACY A 591

Chain	Residue
A	LYS533
A	GLU536

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site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MPD A 592

Chain	Residue
A	PRO200
A	TYR201
A	LYS202

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site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MPD A 593

Chain	Residue
A	GLN246
A	LYS249

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site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ACY A 594

Chain	Residue
A	ASP252

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site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ACY A 595

Chain	Residue
A	TYR531

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site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ACY A 596

Chain	Residue
A	GLU580

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site_id	AC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ACY A 597

Chain	Residue
A	ARG335

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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. PAINWLTSYS

Chain	Residue	Details
A	PRO428-SER437

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