5CDF

Structure at 2.3 A of the alpha/beta monomer of the F-ATPase from Paracoccus denitrificans

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
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	3
Details	binding site for residue GOL A 601

Chain	Residue
A	ASP410
A	LEU411
A	GLN416

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site_id	AC2
Number of Residues	6
Details	binding site for residue GOL A 602

Chain	Residue
A	ASP130
A	VAL131
A	LYS132
A	TYR301
E	ALA60
E	GLU62

---

site_id	AC3
Number of Residues	7
Details	binding site for residue GOL A 603

Chain	Residue
A	ALA177
A	ASP181
A	ARG363
A	PRO364
A	GLN431
A	GLN433
A	HOH712

---

site_id	AC4
Number of Residues	2
Details	binding site for residue GOL A 604

Chain	Residue
A	GLN281
A	HOH718

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site_id	AC5
Number of Residues	6
Details	binding site for residue GOL A 605

Chain	Residue
A	ALA155
A	MET156
A	SER377
A	GLN380
A	LYS392
A	HOH709

---

site_id	AC6
Number of Residues	6
Details	binding site for residue PO4 A 606

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

---

site_id	AC7
Number of Residues	5
Details	binding site for residue GOL E 501

Chain	Residue
E	ILE12
E	VAL15
E	ARG54
E	LEU267
E	LEU268

---

site_id	AC8
Number of Residues	4
Details	binding site for residue GOL E 502

Chain	Residue
A	THR68
E	GLN10
E	ASP17
E	GLY49

---

site_id	AC9
Number of Residues	5
Details	binding site for residue GOL E 503

Chain	Residue
E	ASP83
E	ALA84
E	LEU86
E	ARG88
E	SER207

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PRO364-SER373
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	GLY151

---

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

Chain	Residue	Details
A	SER371

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