Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2XND

Crystal structure of bovine F1-c8 sub-complex of 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	0032559	molecular_function	adenyl ribonucleotide binding
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	1902600	biological_process	proton transmembrane transport
B	0005524	molecular_function	ATP binding
B	0015986	biological_process	proton motive force-driven ATP synthesis
B	0032559	molecular_function	adenyl ribonucleotide binding
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	1902600	biological_process	proton transmembrane transport
C	0005524	molecular_function	ATP binding
C	0015986	biological_process	proton motive force-driven ATP synthesis
C	0032559	molecular_function	adenyl ribonucleotide binding
C	0045261	cellular_component	proton-transporting ATP synthase complex, catalytic core F(1)
C	0046034	biological_process	ATP metabolic process
C	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
C	1902600	biological_process	proton transmembrane transport
D	0005524	molecular_function	ATP binding
D	0015986	biological_process	proton motive force-driven ATP synthesis
D	0016887	molecular_function	ATP hydrolysis activity
D	0045261	cellular_component	proton-transporting ATP synthase complex, catalytic core F(1)
D	0046034	biological_process	ATP metabolic process
D	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
D	1902600	biological_process	proton transmembrane transport
E	0005524	molecular_function	ATP binding
E	0015986	biological_process	proton motive force-driven ATP synthesis
E	0016887	molecular_function	ATP hydrolysis activity
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	1902600	biological_process	proton transmembrane transport
F	0005524	molecular_function	ATP binding
F	0015986	biological_process	proton motive force-driven ATP synthesis
F	0016887	molecular_function	ATP hydrolysis activity
F	0045261	cellular_component	proton-transporting ATP synthase complex, catalytic core F(1)
F	0046034	biological_process	ATP metabolic process
F	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
F	1902600	biological_process	proton transmembrane transport
G	0000275	cellular_component	mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1)
G	0005515	molecular_function	protein binding
G	0005739	cellular_component	mitochondrion
G	0005743	cellular_component	mitochondrial inner membrane
G	0006754	biological_process	ATP biosynthetic process
G	0015986	biological_process	proton motive force-driven ATP synthesis
G	0045259	cellular_component	proton-transporting ATP synthase complex
G	0045261	cellular_component	proton-transporting ATP synthase complex, catalytic core F(1)
G	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
G	1902600	biological_process	proton transmembrane transport
H	0015986	biological_process	proton motive force-driven ATP synthesis
H	0045261	cellular_component	proton-transporting ATP synthase complex, catalytic core F(1)
H	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
I	0000275	cellular_component	mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1)
I	0005739	cellular_component	mitochondrion
I	0005743	cellular_component	mitochondrial inner membrane
I	0006754	biological_process	ATP biosynthetic process
I	0015986	biological_process	proton motive force-driven ATP synthesis
I	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
I	0045259	cellular_component	proton-transporting ATP synthase complex
I	0045261	cellular_component	proton-transporting ATP synthase complex, catalytic core F(1)
I	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
I	1902600	biological_process	proton transmembrane transport
J	0015078	molecular_function	proton transmembrane transporter activity
J	0015986	biological_process	proton motive force-driven ATP synthesis
J	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
J	0045263	cellular_component	proton-transporting ATP synthase complex, coupling factor F(o)
J	1902600	biological_process	proton transmembrane transport
K	0015078	molecular_function	proton transmembrane transporter activity
K	0015986	biological_process	proton motive force-driven ATP synthesis
K	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
K	0045263	cellular_component	proton-transporting ATP synthase complex, coupling factor F(o)
K	1902600	biological_process	proton transmembrane transport
L	0015078	molecular_function	proton transmembrane transporter activity
L	0015986	biological_process	proton motive force-driven ATP synthesis
L	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
L	0045263	cellular_component	proton-transporting ATP synthase complex, coupling factor F(o)
L	1902600	biological_process	proton transmembrane transport
M	0015078	molecular_function	proton transmembrane transporter activity
M	0015986	biological_process	proton motive force-driven ATP synthesis
M	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
M	0045263	cellular_component	proton-transporting ATP synthase complex, coupling factor F(o)
M	1902600	biological_process	proton transmembrane transport
N	0015078	molecular_function	proton transmembrane transporter activity
N	0015986	biological_process	proton motive force-driven ATP synthesis
N	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
N	0045263	cellular_component	proton-transporting ATP synthase complex, coupling factor F(o)
N	1902600	biological_process	proton transmembrane transport
O	0015078	molecular_function	proton transmembrane transporter activity
O	0015986	biological_process	proton motive force-driven ATP synthesis
O	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
O	0045263	cellular_component	proton-transporting ATP synthase complex, coupling factor F(o)
O	1902600	biological_process	proton transmembrane transport
P	0015078	molecular_function	proton transmembrane transporter activity
P	0015986	biological_process	proton motive force-driven ATP synthesis
P	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
P	0045263	cellular_component	proton-transporting ATP synthase complex, coupling factor F(o)
P	1902600	biological_process	proton transmembrane transport
Q	0015078	molecular_function	proton transmembrane transporter activity
Q	0015986	biological_process	proton motive force-driven ATP synthesis
Q	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
Q	0045263	cellular_component	proton-transporting ATP synthase complex, coupling factor F(o)
Q	1902600	biological_process	proton transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ANP A 600

Chain	Residue
A	ARG171
A	PRO363
A	GLN430
A	GLN432
A	MG601
A	GLN172
A	THR173
A	GLY174
A	LYS175
A	THR176
A	SER177
A	PHE357
A	ARG362

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 601

Chain	Residue
A	THR176
A	ASP269
A	ANP600

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ANP B 600

Chain	Residue
B	ARG171
B	GLN172
B	THR173
B	GLY174
B	LYS175
B	THR176
B	SER177
B	PHE357
B	ARG362
B	GLN430
B	GLN432
B	MG601
E	ARG356
E	ASP359

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 601

Chain	Residue
B	THR176
B	ANP600

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 701

Chain	Residue
B	MET62
B	VAL129
B	TYR244
B	TYR248
B	ARG304

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ANP C 600

Chain	Residue
C	ARG171
C	GLN172
C	GLY174
C	LYS175
C	THR176
C	SER177
C	GLU328
C	PHE357
C	ARG362
C	GLN430
C	GLN432
C	MG601
F	TYR368

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 601

Chain	Residue
C	THR176
C	ASP269
C	ANP600

site_id	AC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ANP D 600

Chain	Residue
C	SER344
C	SER372
C	ARG373
D	GLY157
D	ALA158
D	GLY159
D	VAL160
D	GLY161
D	LYS162
D	THR163
D	VAL164
D	GLU188
D	ARG189
D	TYR311
D	TYR345
D	ALA421
D	PHE424
D	THR425
D	MG601

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 601

Chain	Residue
D	THR163
D	GLU188
D	ASP256
D	ANP600

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 E 630

Chain	Residue
A	ARG373
E	LYS162
E	ARG189
E	ASP256
E	ARG260

site_id	BC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ANP F 600

Chain	Residue
F	MG601
B	ILE343
B	SER344
B	ARG373
F	GLY157
F	ALA158
F	GLY159
F	VAL160
F	GLY161
F	LYS162
F	THR163
F	VAL164
F	GLU188
F	ARG189
F	TYR345
F	PHE418
F	ALA421
F	PHE424
F	THR425

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG F 601

Chain	Residue
F	THR163
F	GLU188
F	ARG189
F	GLU192
F	ANP600

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	PRO363-SER372
D	PRO346-SER355

site_id	PS00153
Number of Residues	14
Details	ATPASE_GAMMA ATP synthase gamma subunit signature. ITkEliEiisGAaA

Chain	Residue	Details
G	ILE258-ALA271

site_id	PS00605
Number of Residues	22
Details	ATPASE_C ATP synthase c subunit signature. ARNPslkqqLfSyaILgfaLsE

Chain	Residue	Details
J	ALA37-GLU58

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	320
Details	TRANSMEM: Helical => ECO:0000255

Chain	Residue	Details
J	VAL16-TYR36
N	ILE51-ILE71
O	VAL16-TYR36
O	ILE51-ILE71
P	VAL16-TYR36
P	ILE51-ILE71
Q	VAL16-TYR36
Q	ILE51-ILE71
J	ILE51-ILE71
K	VAL16-TYR36
K	ILE51-ILE71
L	VAL16-TYR36
L	ILE51-ILE71
M	VAL16-TYR36
M	ILE51-ILE71
N	VAL16-TYR36

site_id	SWS_FT_FI2
Number of Residues	8
Details	SITE: Reversibly protonated during proton transport => ECO:0000250

Chain	Residue	Details
J	GLU58
K	GLU58
L	GLU58
M	GLU58
N	GLU58
O	GLU58
P	GLU58
Q	GLU58

site_id	SWS_FT_FI3
Number of Residues	8
Details	MOD_RES: N6,N6,N6-trimethyllysine => ECO:0000250\|UniProtKB:P05496

Chain	Residue	Details
J	LYS43
E	LYS472
F	LYS74
F	LYS111
F	LYS209
F	LYS214
F	LYS472
K	LYS43
L	LYS43
M	LYS43
N	LYS43
O	LYS43
P	LYS43
Q	LYS43
E	LYS214

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:Q91VR2

Chain	Residue	Details
G	LYS90
G	LYS129
E	LYS148
E	LYS376
F	LYS148
F	LYS376

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P36542

Chain	Residue	Details
G	SER121
E	THR262
F	THR262

site_id	SWS_FT_FI6
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P06576

Chain	Residue	Details
D	SER365
B	LYS498
C	LYS80
C	LYS83
C	LYS89
C	LYS197
C	LYS498
E	SER365
F	SER365
A	LYS197
A	LYS498
B	LYS80
B	LYS83
B	LYS89
B	LYS197

site_id	SWS_FT_FI7
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P10719

Chain	Residue	Details
D	SER383
E	SER383
F	SER383

site_id	SWS_FT_FI8
Number of Residues	6
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P56480

Chain	Residue	Details
D	LYS430
A	LYS488
A	LYS496
B	LYS118
B	LYS124
B	LYS187
B	LYS196
B	LYS218
B	LYS262
B	LYS384
B	LYS455
D	LYS435
B	LYS463
B	LYS488
B	LYS496
C	LYS118
C	LYS124
C	LYS187
C	LYS196
C	LYS218
C	LYS262
C	LYS384
E	LYS430
C	LYS455
C	LYS463
C	LYS488
C	LYS496
E	LYS435
F	LYS430
F	LYS435
A	LYS384
A	LYS455
A	LYS463

site_id	SWS_FT_FI9
Number of Residues	3
Details	CARBOHYD: O-linked (GlcNAc) serine => ECO:0000250

Chain	Residue	Details
D	SER56
E	SER56
F	SER56

site_id	SWS_FT_FI10
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P25705

Chain	Residue	Details
A	LYS391
B	LYS391
C	LYS391

site_id	SWS_FT_FI11
Number of Residues	3
Details	CARBOHYD: O-linked (GlcNAc) serine; alternate => ECO:0000250

Chain	Residue	Details
A	SER33
B	SER33
C	SER33

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 178

Chain	Residue	Details
D	LYS162	electrostatic stabiliser
D	GLU188	electrostatic stabiliser
D	ARG189	electrostatic stabiliser

site_id	MCSA2
Number of Residues	3
Details	M-CSA 178

Chain	Residue	Details
E	LYS162	electrostatic stabiliser
E	GLU188	electrostatic stabiliser
E	ARG189	electrostatic stabiliser

site_id	MCSA3
Number of Residues	3
Details	M-CSA 178

Chain	Residue	Details
F	LYS162	electrostatic stabiliser
F	GLU188	electrostatic stabiliser
F	ARG189	electrostatic stabiliser

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)