Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6ZQN

bovine ATP synthase monomer state 3 (combined)

Functional Information from GO Data

Chain	GOid	namespace	contents
8	0005739	cellular_component	mitochondrion
8	0006754	biological_process	ATP biosynthetic process
8	0006811	biological_process	monoatomic ion transport
8	0015078	molecular_function	proton transmembrane transporter activity
8	0015986	biological_process	proton motive force-driven ATP synthesis
8	0031966	cellular_component	mitochondrial membrane
8	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
8	0045259	cellular_component	proton-transporting ATP synthase complex
8	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
8	1902600	biological_process	proton transmembrane transport
a	0005743	cellular_component	mitochondrial inner membrane
a	0006754	biological_process	ATP biosynthetic process
a	0006811	biological_process	monoatomic ion transport
a	0015078	molecular_function	proton transmembrane transporter activity
a	0015252	molecular_function	proton channel activity
a	0015986	biological_process	proton motive force-driven ATP synthesis
a	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
a	0045259	cellular_component	proton-transporting ATP synthase complex
a	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
a	1902600	biological_process	proton transmembrane transport
A	0000166	molecular_function	nucleotide binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
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	0006811	biological_process	monoatomic ion transport
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	0046034	biological_process	ATP metabolic process
A	0046872	molecular_function	metal ion binding
A	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
A	1902600	biological_process	proton transmembrane transport
b	0015078	molecular_function	proton transmembrane transporter activity
b	0015986	biological_process	proton motive force-driven ATP synthesis
B	0000166	molecular_function	nucleotide binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
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	0006811	biological_process	monoatomic ion transport
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	0046034	biological_process	ATP metabolic process
B	0046872	molecular_function	metal ion binding
B	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
B	1902600	biological_process	proton transmembrane transport
C	0000166	molecular_function	nucleotide binding
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
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	0006811	biological_process	monoatomic ion transport
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	0046034	biological_process	ATP metabolic process
C	0046872	molecular_function	metal ion binding
C	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
C	1902600	biological_process	proton transmembrane transport
d	0005739	cellular_component	mitochondrion
d	0005743	cellular_component	mitochondrial inner membrane
d	0006811	biological_process	monoatomic ion transport
d	0015078	molecular_function	proton transmembrane transporter activity
d	0015986	biological_process	proton motive force-driven ATP synthesis
d	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
d	0045259	cellular_component	proton-transporting ATP synthase complex
d	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
d	1902600	biological_process	proton transmembrane transport
D	0000166	molecular_function	nucleotide binding
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	0006811	biological_process	monoatomic ion transport
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	0046034	biological_process	ATP metabolic process
D	0046872	molecular_function	metal ion binding
D	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
D	1902600	biological_process	proton transmembrane transport
e	0005739	cellular_component	mitochondrion
e	0005743	cellular_component	mitochondrial inner membrane
e	0006754	biological_process	ATP biosynthetic process
e	0006811	biological_process	monoatomic ion transport
e	0015078	molecular_function	proton transmembrane transporter activity
e	0015986	biological_process	proton motive force-driven ATP synthesis
e	0016020	cellular_component	membrane
e	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
e	0045259	cellular_component	proton-transporting ATP synthase complex
e	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
e	1902600	biological_process	proton transmembrane transport
E	0000166	molecular_function	nucleotide binding
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	0006811	biological_process	monoatomic ion transport
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	0046034	biological_process	ATP metabolic process
E	0046872	molecular_function	metal ion binding
E	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
E	1902600	biological_process	proton transmembrane transport
f	0005739	cellular_component	mitochondrion
f	0005743	cellular_component	mitochondrial inner membrane
f	0006754	biological_process	ATP biosynthetic process
f	0006811	biological_process	monoatomic ion transport
f	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
f	0045259	cellular_component	proton-transporting ATP synthase complex
f	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
f	1902600	biological_process	proton transmembrane transport
F	0000166	molecular_function	nucleotide binding
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	0006811	biological_process	monoatomic ion transport
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	0046034	biological_process	ATP metabolic process
F	0046872	molecular_function	metal ion binding
F	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
F	1902600	biological_process	proton transmembrane transport
g	0005739	cellular_component	mitochondrion
g	0005743	cellular_component	mitochondrial inner membrane
g	0006754	biological_process	ATP biosynthetic process
g	0006811	biological_process	monoatomic ion transport
g	0015078	molecular_function	proton transmembrane transporter activity
g	0015986	biological_process	proton motive force-driven ATP synthesis
g	0045259	cellular_component	proton-transporting ATP synthase complex
g	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
g	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	0006811	biological_process	monoatomic ion transport
G	0015986	biological_process	proton motive force-driven ATP synthesis
G	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
G	0045259	cellular_component	proton-transporting ATP synthase complex
G	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
G	1902600	biological_process	proton transmembrane transport
h	0015078	molecular_function	proton transmembrane transporter activity
h	0015986	biological_process	proton motive force-driven ATP synthesis
h	0045259	cellular_component	proton-transporting ATP synthase complex
H	0015986	biological_process	proton motive force-driven ATP synthesis
H	0045259	cellular_component	proton-transporting ATP synthase complex
H	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
I	0005739	cellular_component	mitochondrion
I	0005743	cellular_component	mitochondrial inner membrane
I	0006754	biological_process	ATP biosynthetic process
I	0006811	biological_process	monoatomic ion transport
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	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
I	1902600	biological_process	proton transmembrane transport
j	0005739	cellular_component	mitochondrion
j	0031966	cellular_component	mitochondrial membrane
j	0045259	cellular_component	proton-transporting ATP synthase complex
J	0005739	cellular_component	mitochondrion
J	0032780	biological_process	negative regulation of ATP-dependent activity
J	0042030	molecular_function	ATPase inhibitor activity
k	0005739	cellular_component	mitochondrion
k	0031966	cellular_component	mitochondrial membrane
k	0045259	cellular_component	proton-transporting ATP synthase complex
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	0045259	cellular_component	proton-transporting ATP synthase complex
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	0045259	cellular_component	proton-transporting ATP synthase complex
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	0045259	cellular_component	proton-transporting ATP synthase complex
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	0045259	cellular_component	proton-transporting ATP synthase complex
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	0045259	cellular_component	proton-transporting ATP synthase complex
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	0045259	cellular_component	proton-transporting ATP synthase complex
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	0045259	cellular_component	proton-transporting ATP synthase complex
Q	1902600	biological_process	proton transmembrane transport
R	0015078	molecular_function	proton transmembrane transporter activity
R	0015986	biological_process	proton motive force-driven ATP synthesis
R	0033177	cellular_component	proton-transporting two-sector ATPase complex, proton-transporting domain
R	0045259	cellular_component	proton-transporting ATP synthase complex
R	1902600	biological_process	proton transmembrane transport
S	0015986	biological_process	proton motive force-driven ATP synthesis
S	0016020	cellular_component	membrane
S	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue ATP A 600

Chain	Residue
A	GLN172
A	GLY431
A	GLN432
A	MG601
A	HOH702
A	HOH703
D	TYR368
A	THR173
A	GLY174
A	LYS175
A	THR176
A	SER177
A	PHE357
A	ARG362
A	GLN430

site_id	AC2
Number of Residues	5
Details	binding site for residue MG A 601

Chain	Residue
A	THR176
A	ATP600
A	HOH701
A	HOH702
A	HOH703

site_id	AC3
Number of Residues	16
Details	binding site for residue ATP B 600

Chain	Residue
B	GLN172
B	THR173
B	GLY174
B	LYS175
B	THR176
B	SER177
B	PHE357
B	ARG362
B	GLN430
B	GLY431
B	GLN432
B	MG601
B	HOH701
B	HOH703
E	ARG356
E	ASP359

site_id	AC4
Number of Residues	5
Details	binding site for residue MG B 601

Chain	Residue
B	THR176
B	ATP600
B	HOH701
B	HOH702
B	HOH703

site_id	AC5
Number of Residues	19
Details	binding site for residue ATP C 600

Chain	Residue
C	GLN172
C	THR173
C	GLY174
C	LYS175
C	THR176
C	SER177
C	GLU328
C	ARG362
C	PRO363
C	GLN430
C	GLY431
C	GLN432
C	MG601
C	HOH701
C	HOH702
C	HOH703
F	ARG356
F	ASP359
F	TYR368

site_id	AC6
Number of Residues	5
Details	binding site for residue MG C 601

Chain	Residue
C	THR176
C	ATP600
C	HOH701
C	HOH702
C	HOH703

site_id	AC7
Number of Residues	13
Details	binding site for residue ADP D 600

Chain	Residue
C	ARG373
D	ALA158
D	GLY159
D	GLY161
D	LYS162
D	THR163
D	VAL164
D	TYR345
D	PHE418
D	THR425
D	MG601
D	HOH702
D	HOH703

site_id	AC8
Number of Residues	8
Details	binding site for residue MG D 601

Chain	Residue
D	THR163
D	GLU188
D	GLU192
D	ADP600
D	HOH701
D	HOH702
D	HOH703
D	HOH704

site_id	AC9
Number of Residues	10
Details	binding site for residue ADP E 600

Chain	Residue
E	ALA158
E	GLY159
E	VAL160
E	GLY161
E	LYS162
E	THR163
E	VAL164
E	TYR345
E	PHE418
E	PHE424

site_id	AD1
Number of Residues	14
Details	binding site for residue ADP F 600

Chain	Residue
F	VAL160
F	GLY161
F	LYS162
F	THR163
F	VAL164
F	TYR345
F	PHE418
F	ALA421
F	MG601
F	HOH701
F	HOH702
B	ARG373
F	ALA158
F	GLY159

site_id	AD2
Number of Residues	9
Details	binding site for residue MG F 601

Chain	Residue
F	THR163
F	GLU188
F	ARG189
F	GLU192
F	ADP600
F	HOH701
F	HOH702
F	HOH703
F	HOH704

site_id	AD3
Number of Residues	11
Details	binding site for residue CDL f 101

Chain	Residue
8	ILE22
8	LYS27
a	LEU22
a	PHE26
a	LEU29
a	PRO32
a	THR33
f	GLN38
f	TYR41
f	TYR42
j	LYS8

site_id	AD4
Number of Residues	6
Details	binding site for residue LHG f 102

Chain	Residue
b	CDL301
f	LYS10
f	LEU11
f	LEU12
f	ARG39
f	ARG43

site_id	AD5
Number of Residues	6
Details	binding site for residue LHG f 103

Chain	Residue
b	CDL301
f	PHE68
f	TYR71
f	CYS72
f	TYR75
f	LYS79

site_id	AD6
Number of Residues	17
Details	binding site for residue CDL b 301

Chain	Residue
a	LEU29
b	GLU20
b	PHE21
b	PHE24
f	LEU12
f	GLY40
f	TYR41
f	ARG43
f	TYR44
f	LYS47
f	TYR48
f	VAL49
f	VAL62
f	PHE68
f	LHG102
f	LHG103
g	LYS70

site_id	AD7
Number of Residues	17
Details	binding site for residue CDL b 302

Chain	Residue
a	ARG41
a	PHE42
a	LEU45
a	GLN46
a	LEU85
a	MET208
b	PHE14
b	LEU67
b	VAL68
b	VAL71
b	LYS72
b	GLY75
b	VAL78
f	GLY54
f	SER55
f	ILE56
f	LEU63

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	PS00389
Number of Residues	20
Details	ATPASE_DELTA ATP synthase delta (OSCP) subunit signature. LkLevkIDpSImGGMIVRiG

Chain	Residue	Details
S	LEU148-GLY167

site_id	PS00449
Number of Residues	10
Details	ATPASE_A ATP synthase a subunit signature. ALAVRLTANI

Chain	Residue	Details
a	ALA155-ILE164

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

Chain	Residue	Details
Q	ALA37-GLU58

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17895376","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8065448","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8790345","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9687365","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BMF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1COW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E1Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E1R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1E79","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EFR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1H8H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NBM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OHH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CK3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JDI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JIZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JJ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JJ2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2V7Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WSS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XND","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TSF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TT3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YXW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Z1M","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	3
Details	Site: {"description":"Required for activity","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	10
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine; alternate","evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	15
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	3
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P15999","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	33
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	3
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	3
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine; alternate","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	15
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17895376","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9687365","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NBM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2V7Q","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9687365","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NBM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PDB","id":"1E1R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1H8E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ASU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TSF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	15
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P56480","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06576","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	3
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P56480","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06576","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P10719","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56480","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	3
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91VR2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q91VR2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P36542","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q91VR2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P36542","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9D3D9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	3
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P56382","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56382","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	2
Details	Site: {"description":"Participates in pH sensing"}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	418
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	8
Details	Site: {"description":"Reversibly protonated during proton transport","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	8
Details	Modified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"UniProtKB","id":"Q06055","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	5
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DB20","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9DB20","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI36
Number of Residues	3
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9DB20","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI37
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P48047","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI38
Number of Residues	1
Details	Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"1827992","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2875870","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI39
Number of Residues	1
Details	Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"2875870","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI40
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DCX2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI41
Number of Residues	5
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9DCX2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI42
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O75947","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI43
Number of Residues	17
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P56134","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI44
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P56135","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI45
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O75964","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI46
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CPQ8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI47
Number of Residues	17
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P56378","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI48
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQQ7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI49
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQQ7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI50
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P24539","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI51
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P18859","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI52
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P97450","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI53
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P97450","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI54
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; partial","evidences":[{"source":"UniProtKB","id":"Q78IK2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI55
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q06185","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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)