1SKY

CRYSTAL STRUCTURE OF THE NUCLEOTIDE FREE ALPHA3BETA3 SUB-COMPLEX OF F1-ATPASE FROM THE THERMOPHILIC BACILLUS PS3

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0005524	molecular_function	ATP binding
B	0005886	cellular_component	plasma membrane
B	0006754	biological_process	ATP biosynthetic process
B	0015986	biological_process	proton motive force-driven ATP synthesis
B	0032559	molecular_function	adenyl ribonucleotide binding
B	0043531	molecular_function	ADP binding
B	0045259	cellular_component	proton-transporting ATP synthase complex
B	0045261	cellular_component	proton-transporting ATP synthase complex, catalytic core F(1)
B	0046034	biological_process	ATP metabolic process
B	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
B	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
B	1902600	biological_process	proton transmembrane transport
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005886	cellular_component	plasma membrane
E	0006754	biological_process	ATP biosynthetic process
E	0015986	biological_process	proton motive force-driven ATP synthesis
E	0016887	molecular_function	ATP hydrolysis activity
E	0045259	cellular_component	proton-transporting ATP synthase complex
E	0045261	cellular_component	proton-transporting ATP synthase complex, catalytic core F(1)
E	0046034	biological_process	ATP metabolic process
E	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
E	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
E	1902600	biological_process	proton transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 503

Chain	Residue
B	ASP170
B	GLN172
B	THR173
B	GLY174
B	LYS175
B	THR176

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 E 474

Chain	Residue
E	GLY161
E	VAL162
E	GLY163
E	LYS164
E	THR165
E	GLY159
E	ALA160

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site_id	CAT
Number of Residues	1
Details	THE CARBOXYLATE GROUP OF THE GLUTAMIC ACID RESIDUE IS BELIEVED TO ACTIVATE A WATER MOLECULE FOR INLINE ATTACK ON THE GAMMA PHOSPHATE DURING ATP HYDROLYSIS. THE ARGININE RESIDUE (WHICH IS LOCATED ON AN ADJACENT ALPHA SUBUNIT) COULD HELP TO STABILIZE THE NEGATIVE CHARGE THAT DEVELOPS ON THE TERMINAL PHOSPHATE IN THE PUTATIVE PENTACOORDINATED TRANSITION STATE.

Chain	Residue
E	GLU190

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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. PAINAGLSVS

Chain	Residue	Details
B	PRO355-SER364
E	PRO342-SER351

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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
E	GLY158

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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
B	SER362

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
E	LYS164
E	ARG191
E	GLU190

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

Chain	Residue	Details
B	ARG365

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site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
E	ARG352

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site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
B	LYS175
B	LYS201
B	GLN200

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