Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2JJ2

The Structure of F1-ATPase inhibited by quercetin.

Functional Information from GO Data

Chain	GOid	namespace	contents
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	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	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	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	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	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	0000166	molecular_function	nucleotide binding
H	0005515	molecular_function	protein binding
H	0005524	molecular_function	ATP binding
H	0005739	cellular_component	mitochondrion
H	0005743	cellular_component	mitochondrial inner membrane
H	0005886	cellular_component	plasma membrane
H	0006754	biological_process	ATP biosynthetic process
H	0006811	biological_process	monoatomic ion transport
H	0015986	biological_process	proton motive force-driven ATP synthesis
H	0032559	molecular_function	adenyl ribonucleotide binding
H	0043531	molecular_function	ADP binding
H	0045259	cellular_component	proton-transporting ATP synthase complex
H	0046034	biological_process	ATP metabolic process
H	0046872	molecular_function	metal ion binding
H	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
H	1902600	biological_process	proton transmembrane transport
I	0000166	molecular_function	nucleotide binding
I	0005515	molecular_function	protein binding
I	0005524	molecular_function	ATP binding
I	0005739	cellular_component	mitochondrion
I	0005743	cellular_component	mitochondrial inner membrane
I	0005886	cellular_component	plasma 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	0032559	molecular_function	adenyl ribonucleotide binding
I	0043531	molecular_function	ADP binding
I	0045259	cellular_component	proton-transporting ATP synthase complex
I	0046034	biological_process	ATP metabolic process
I	0046872	molecular_function	metal ion binding
I	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
I	1902600	biological_process	proton transmembrane transport
J	0000166	molecular_function	nucleotide binding
J	0005515	molecular_function	protein binding
J	0005524	molecular_function	ATP binding
J	0005739	cellular_component	mitochondrion
J	0005743	cellular_component	mitochondrial inner membrane
J	0005886	cellular_component	plasma membrane
J	0006754	biological_process	ATP biosynthetic process
J	0006811	biological_process	monoatomic ion transport
J	0015986	biological_process	proton motive force-driven ATP synthesis
J	0032559	molecular_function	adenyl ribonucleotide binding
J	0043531	molecular_function	ADP binding
J	0045259	cellular_component	proton-transporting ATP synthase complex
J	0046034	biological_process	ATP metabolic process
J	0046872	molecular_function	metal ion binding
J	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
J	1902600	biological_process	proton transmembrane transport
K	0000166	molecular_function	nucleotide binding
K	0005515	molecular_function	protein binding
K	0005524	molecular_function	ATP binding
K	0005737	cellular_component	cytoplasm
K	0005739	cellular_component	mitochondrion
K	0005743	cellular_component	mitochondrial inner membrane
K	0006754	biological_process	ATP biosynthetic process
K	0006811	biological_process	monoatomic ion transport
K	0015986	biological_process	proton motive force-driven ATP synthesis
K	0016887	molecular_function	ATP hydrolysis activity
K	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
K	0045259	cellular_component	proton-transporting ATP synthase complex
K	0046034	biological_process	ATP metabolic process
K	0046872	molecular_function	metal ion binding
K	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
K	1902600	biological_process	proton transmembrane transport
L	0000166	molecular_function	nucleotide binding
L	0005515	molecular_function	protein binding
L	0005524	molecular_function	ATP binding
L	0005737	cellular_component	cytoplasm
L	0005739	cellular_component	mitochondrion
L	0005743	cellular_component	mitochondrial inner membrane
L	0006754	biological_process	ATP biosynthetic process
L	0006811	biological_process	monoatomic ion transport
L	0015986	biological_process	proton motive force-driven ATP synthesis
L	0016887	molecular_function	ATP hydrolysis activity
L	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
L	0045259	cellular_component	proton-transporting ATP synthase complex
L	0046034	biological_process	ATP metabolic process
L	0046872	molecular_function	metal ion binding
L	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
L	1902600	biological_process	proton transmembrane transport
M	0000166	molecular_function	nucleotide binding
M	0005515	molecular_function	protein binding
M	0005524	molecular_function	ATP binding
M	0005737	cellular_component	cytoplasm
M	0005739	cellular_component	mitochondrion
M	0005743	cellular_component	mitochondrial inner membrane
M	0006754	biological_process	ATP biosynthetic process
M	0006811	biological_process	monoatomic ion transport
M	0015986	biological_process	proton motive force-driven ATP synthesis
M	0016887	molecular_function	ATP hydrolysis activity
M	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
M	0045259	cellular_component	proton-transporting ATP synthase complex
M	0046034	biological_process	ATP metabolic process
M	0046872	molecular_function	metal ion binding
M	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
M	1902600	biological_process	proton transmembrane transport
N	0005515	molecular_function	protein binding
N	0005739	cellular_component	mitochondrion
N	0005743	cellular_component	mitochondrial inner membrane
N	0006754	biological_process	ATP biosynthetic process
N	0006811	biological_process	monoatomic ion transport
N	0015986	biological_process	proton motive force-driven ATP synthesis
N	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
N	0045259	cellular_component	proton-transporting ATP synthase complex
N	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
N	1902600	biological_process	proton transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ANP A 1511

Chain	Residue
A	ARG171
A	GLN430
A	GLN432
A	MG1512
A	HOH2173
A	HOH2174
A	HOH2175
A	HOH2176
A	HOH2177
A	HOH2179
A	HOH2180
A	GLN172
D	HOH2154
A	THR173
A	GLY174
A	LYS175
A	THR176
A	SER177
A	PHE357
A	PRO363

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1512

Chain	Residue
A	THR176
A	ANP1511
A	HOH2060
A	HOH2093
A	HOH2175

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 1513

Chain	Residue
A	GLY130
A	TYR244
A	LEU245
A	TYR248
A	ARG304

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1514

Chain	Residue
A	ARG291
A	TYR294
A	PRO295
A	GLY296
A	TYR337
E	SER266
E	GLY280

site_id	AC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ANP B 1510

Chain	Residue
B	ARG171
B	GLN172
B	THR173
B	GLY174
B	LYS175
B	THR176
B	SER177
B	PHE357
B	ARG362
B	GLN430
B	GLY431
B	GLN432
B	MG1511
B	HOH2075
B	HOH2148
B	HOH2149
B	HOH2151
E	ARG356
E	ASP359

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 1511

Chain	Residue
B	THR176
B	ANP1510
B	HOH2055
B	HOH2075
B	HOH2149

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 1512

Chain	Residue
B	VAL129
B	GLY130
B	TYR244
B	TYR248
B	ARG304
B	HOH2152
B	HOH2153

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 1513

Chain	Residue
B	GLY290
B	ARG291
B	TYR294
B	TYR337
B	HOH2090
F	SER266
F	VAL279

site_id	AC9
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ANP C 1511

Chain	Residue
C	ARG171
C	GLN172
C	THR173
C	GLY174
C	LYS175
C	THR176
C	SER177
C	PHE357
C	ARG362
C	GLN430
C	GLN432
C	MG1512
C	HOH2073
C	HOH2108
C	HOH2222
C	HOH2223
C	HOH2224
C	HOH2225
C	HOH2226
C	HOH2227
C	HOH2228
F	TYR368

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 1512

Chain	Residue
C	HOH2076
C	HOH2108
C	HOH2224
C	THR176
C	ANP1511

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 1513

Chain	Residue
C	MET62
C	VAL129
C	GLY130
C	TYR244
C	TYR248
C	ARG304
C	HOH2229

site_id	BC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ADP D 1476

Chain	Residue
C	SER372
C	ARG373
D	GLY157
D	GLY159
D	VAL160
D	GLY161
D	LYS162
D	THR163
D	VAL164
D	TYR345
D	PHE418
D	ALA421
D	PHE424
D	THR425
D	MG1477
D	AZI1478
D	HOH2071
D	HOH2175
D	HOH2176
D	HOH2177
D	HOH2178

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG D 1477

Chain	Residue
D	THR163
D	ASP256
D	ADP1476
D	HOH2069
D	HOH2071
D	HOH2093
D	HOH2176

site_id	BC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE AZI D 1478

Chain	Residue
C	SER344
C	ARG373
C	HOH2153
D	ALA158
D	GLY159
D	LYS162
D	TYR311
D	ADP1476
D	HOH2176
D	HOH2179

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL D 1479

Chain	Residue
D	ARG231
D	GLY265
D	ARG274

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 E 1475

Chain	Residue
E	GLY157
E	ALA158
E	GLY159
E	LYS162
E	THR163
E	HOH2043
E	HOH2044

site_id	BC8
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ANP F 1475

Chain	Residue
B	ILE343
B	SER344
B	VAL371
B	ARG373
F	ALA158
F	GLY159
F	VAL160
F	GLY161
F	LYS162
F	THR163
F	VAL164
F	ARG189
F	TYR345
F	PHE418
F	ALA421
F	PHE424
F	THR425
F	MG1476
F	HOH2079
F	HOH2100
F	HOH2202
F	HOH2203
F	HOH2204
F	HOH2205

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG F 1476

Chain	Residue
F	THR163
F	ANP1475
F	HOH2079
F	HOH2100
F	HOH2202

site_id	CC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE QUE G 1273

Chain	Residue
B	ARG291
B	GLU292
B	HOH2091
C	GLU292
C	ALA293
F	VAL279
F	HOH2139
G	ALA256
G	THR259
G	LYS260
G	ILE263
G	HOH2039
G	HOH2040

site_id	CC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ANP H 1511

Chain	Residue
H	ARG171
H	GLN172
H	THR173
H	GLY174
H	LYS175
H	THR176
H	SER177
H	PHE357
H	ARG362
H	PRO363
H	GLN430
H	GLN432
H	MG1512
H	HOH2070
H	HOH2071
H	HOH2131
H	HOH2196
H	HOH2197
H	HOH2198
H	HOH2199
H	HOH2200
H	HOH2201
H	HOH2202
H	HOH2204
H	HOH2205

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG H 1512

Chain	Residue
H	THR176
H	ANP1511
H	HOH2071
H	HOH2196
H	HOH2197

site_id	CC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL H 1513

Chain	Residue
H	GLY130
H	TYR244
H	LEU245
H	TYR248
H	ARG304
H	HOH2206
H	HOH2207

site_id	CC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL H 1514

Chain	Residue
H	GLY290
H	ARG291
H	TYR294
H	PRO295
H	GLY296
H	TYR337
L	SER266
L	GLU267
L	GLY280
L	HOH2067

site_id	CC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ANP I 1510

Chain	Residue
I	ARG171
I	GLN172
I	THR173
I	GLY174
I	LYS175
I	THR176
I	SER177
I	PHE357
I	ARG362
I	GLN430
I	GLN432
I	MG1511
I	HOH2079
I	HOH2114
I	HOH2150
I	HOH2151
L	ARG356
L	ASP359

site_id	CC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG I 1511

Chain	Residue
I	THR176
I	ANP1510
I	HOH2053
I	HOH2079
I	HOH2150

site_id	CC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL I 1512

Chain	Residue
I	VAL129
I	GLY130
I	TYR244
I	TYR248
I	ARG304
I	HOH2152
I	HOH2153

site_id	CC9
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ANP J 1511

Chain	Residue
J	ARG171
J	GLN172
J	THR173
J	GLY174
J	LYS175
J	THR176
J	SER177
J	PHE357
J	ARG362
J	GLN430
J	GLN432
J	MG1512
J	HOH2082
J	HOH2122
J	HOH2228
J	HOH2230
J	HOH2231
J	HOH2232
J	HOH2233
J	HOH2234
M	TYR368
M	HOH2166
M	HOH2171

site_id	DC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG J 1512

Chain	Residue
J	THR176
J	ANP1511
J	HOH2086
J	HOH2122
J	HOH2228

site_id	DC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL J 1513

Chain	Residue
J	MET62
J	VAL129
J	GLY130
J	TYR244
J	TYR248
J	ARG304
J	HOH2149
J	HOH2235
J	HOH2236

site_id	DC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ADP K 1476

Chain	Residue
J	SER372
J	ARG373
K	GLY159
K	VAL160
K	GLY161
K	LYS162
K	THR163
K	VAL164
K	TYR345
K	PHE418
K	ALA421
K	PHE424
K	THR425
K	MG1477
K	AZI1478
K	HOH2153
K	HOH2172
K	HOH2173
K	HOH2174

site_id	DC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG K 1477

Chain	Residue
K	THR163
K	ADP1476
K	HOH2062
K	HOH2083
K	HOH2172
K	HOH2173

site_id	DC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE AZI K 1478

Chain	Residue
J	SER344
J	ARG373
K	ALA158
K	GLY159
K	LYS162
K	ARG189
K	TYR311
K	ADP1476
K	HOH2063
K	HOH2064
K	HOH2172

site_id	DC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL K 1479

Chain	Residue
K	ARG231
K	GLY265
K	ARG274
K	THR284
K	ASP288

site_id	DC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL K 1480

Chain	Residue
H	GLN215
K	SER127
K	GLU129
K	GLY150
K	HOH2175

site_id	DC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 L 1475

Chain	Residue
L	GLY157
L	ALA158
L	GLY159
L	VAL160
L	GLY161
L	LYS162
L	THR163
L	HOH2121
L	HOH2122

site_id	DC9
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ANP M 1475

Chain	Residue
I	ILE343
I	SER344
I	VAL371
I	ARG373
M	ALA158
M	GLY159
M	VAL160
M	GLY161
M	LYS162
M	THR163
M	VAL164
M	GLU188
M	ARG189
M	TYR345
M	PHE418
M	ALA421
M	PHE424
M	THR425
M	MG1476
M	HOH2078
M	HOH2104
M	HOH2199
M	HOH2200
M	HOH2201
M	HOH2202

site_id	EC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG M 1476

Chain	Residue
M	THR163
M	ANP1475
M	HOH2078
M	HOH2104
M	HOH2199

site_id	EC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE QUE N 1273

Chain	Residue
I	ARG291
I	GLU292
J	GLU292
M	ALA278
M	VAL279
N	ALA256
N	THR259
N	LYS260
N	ILE263
N	HOH2037
N	HOH2038
N	HOH2039

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
D	PRO346-SER355
A	PRO363-SER372

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	48
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	6
Details	Site: {"description":"Required for activity","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine; alternate","evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	30
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P15999","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	66
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q03265","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	14
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P25705","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	6
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	6
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	6
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine; alternate","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	30
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	12
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	6
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	30
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	12
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	6
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P56480","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06576","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P10719","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	12
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	6
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	2
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	4
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	4
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

Catalytic Information from CSA

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

Chain	Residue	Details
D	ARG356

site_id	CSA10
Number of Residues	4
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
J	ARG373
K	ARG189
K	GLU188
K	LYS162

site_id	CSA11
Number of Residues	4
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
H	ARG373
L	ARG189
L	GLU188
L	LYS162

site_id	CSA12
Number of Residues	4
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
M	ARG189
M	GLU188
M	LYS162
I	ARG373

site_id	CSA13
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
A	LYS175
A	LYS209
A	GLN208

site_id	CSA14
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
B	LYS175
B	LYS209
B	GLN208

site_id	CSA15
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
C	LYS175
C	LYS209
C	GLN208

site_id	CSA16
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
H	LYS175
H	LYS209
H	GLN208

site_id	CSA17
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
I	LYS175
I	LYS209
I	GLN208

site_id	CSA18
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
J	LYS175
J	LYS209
J	GLN208

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

Chain	Residue	Details
E	ARG356

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

Chain	Residue	Details
F	ARG356

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

Chain	Residue	Details
K	ARG356

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

Chain	Residue	Details
L	ARG356

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

Chain	Residue	Details
M	ARG356

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
C	ARG373
D	ARG189
D	GLU188
D	LYS162

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
A	ARG373
E	ARG189
E	GLU188
E	LYS162

site_id	CSA9
Number of Residues	4
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
F	ARG189
F	GLU188
F	LYS162
B	ARG373

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

site_id	MCSA4
Number of Residues	3
Details	M-CSA 178

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

site_id	MCSA5
Number of Residues	3
Details	M-CSA 178

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

site_id	MCSA6
Number of Residues	3
Details	M-CSA 178

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

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