Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2W6F

Low resolution structures of bovine mitochondrial F1-ATPase during controlled dehydration: Hydration State 2.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
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	0045267	cellular_component	proton-transporting ATP synthase, catalytic core
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	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005743	cellular_component	mitochondrial inner membrane
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	0045267	cellular_component	proton-transporting ATP synthase, catalytic core
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	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005743	cellular_component	mitochondrial inner membrane
C	0005886	cellular_component	plasma membrane
C	0006754	biological_process	ATP biosynthetic process
C	0015986	biological_process	proton motive force-driven ATP synthesis
C	0032559	molecular_function	adenyl ribonucleotide binding
C	0043531	molecular_function	ADP binding
C	0045259	cellular_component	proton-transporting ATP synthase complex
C	0045261	cellular_component	proton-transporting ATP synthase complex, catalytic core F(1)
C	0045267	cellular_component	proton-transporting ATP synthase, catalytic core
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	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005743	cellular_component	mitochondrial inner membrane
D	0006754	biological_process	ATP biosynthetic process
D	0015986	biological_process	proton motive force-driven ATP synthesis
D	0016887	molecular_function	ATP hydrolysis activity
D	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
D	0045259	cellular_component	proton-transporting ATP synthase complex
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	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
D	1902600	biological_process	proton transmembrane transport
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005739	cellular_component	mitochondrion
E	0005743	cellular_component	mitochondrial inner 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	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
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
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005739	cellular_component	mitochondrion
F	0005743	cellular_component	mitochondrial inner membrane
F	0006754	biological_process	ATP biosynthetic process
F	0015986	biological_process	proton motive force-driven ATP synthesis
F	0016887	molecular_function	ATP hydrolysis activity
F	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
F	0045259	cellular_component	proton-transporting ATP synthase complex
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	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
F	1902600	biological_process	proton transmembrane transport
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

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

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:Q91VR2

Chain	Residue	Details
G	LYS14
E	GLY157
F	GLY157
B	GLN430
C	ASP170
C	GLN430

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:Q91VR2

Chain	Residue	Details
G	LYS24
G	LYS245
F	ARG189

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P36542

Chain	Residue	Details
G	LYS30
E	LYS472
F	LYS74
F	LYS111
F	LYS209
F	LYS214
F	LYS472
G	LYS172
D	LYS209
D	LYS214
D	LYS472
E	LYS74
E	LYS111
E	LYS209
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
C	SER22
C	SER123
C	SER141
G	LYS129
E	LYS148
E	LYS376
F	LYS148
F	LYS376
B	SER123
B	SER141
C	SER10

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
E	SER365
F	SER365

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

Chain	Residue	Details
D	SER383
B	LYS498
C	LYS80
C	LYS83
C	LYS89
C	LYS197
C	LYS498
E	SER383
F	SER383
A	LYS197
A	LYS498
B	LYS80
B	LYS83
B	LYS89
B	LYS197

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

Chain	Residue	Details
D	LYS430
D	LYS435
E	LYS430
E	LYS435
F	LYS430
F	LYS435

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

Chain	Residue	Details
D	SER56
A	LYS488
A	LYS496
B	LYS118
B	LYS124
B	LYS187
B	LYS196
B	LYS218
B	LYS262
B	LYS384
B	LYS455
E	SER56
B	LYS463
B	LYS488
B	LYS496
C	LYS118
C	LYS124
C	LYS187
C	LYS196
C	LYS218
C	LYS262
C	LYS384
F	SER56
C	LYS455
C	LYS463
C	LYS488
C	LYS496
A	LYS196
A	LYS218
A	LYS262
A	LYS384
A	LYS455
A	LYS463

site_id	SWS_FT_FI10
Number of Residues	3
Details	MOD_RES: Omega-N-methylarginine => ECO:0000250\|UniProtKB:Q03265

Chain	Residue	Details
A	ARG161
B	ARG161
C	ARG161

site_id	SWS_FT_FI11
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_FI12
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	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
A	ARG373

site_id	CSA10
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
A	LYS175
A	LYS209
A	GLN208

site_id	CSA11
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
B	LYS175
B	LYS209
B	GLN208

site_id	CSA12
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
C	LYS175
C	LYS209
C	GLN208

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

Chain	Residue	Details
B	ARG373

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

Chain	Residue	Details
C	ARG373

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

Chain	Residue	Details
D	ARG356

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
E	ARG356

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
F	ARG356

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
D	ARG189
D	LYS162
D	GLU188

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
E	ARG189
E	LYS162
E	GLU188

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
F	ARG189
F	LYS162
F	GLU188

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)