Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1M34

Nitrogenase Complex From Azotobacter Vinelandii Stabilized By ADP-Tetrafluoroaluminate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0009399	biological_process	nitrogen fixation
A	0016163	molecular_function	nitrogenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0016612	cellular_component	molybdenum-iron nitrogenase complex
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
B	0000166	molecular_function	nucleotide binding
B	0005524	molecular_function	ATP binding
B	0009399	biological_process	nitrogen fixation
B	0016163	molecular_function	nitrogenase activity
B	0016491	molecular_function	oxidoreductase activity
B	0016612	cellular_component	molybdenum-iron nitrogenase complex
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
C	0000166	molecular_function	nucleotide binding
C	0005524	molecular_function	ATP binding
C	0009399	biological_process	nitrogen fixation
C	0016163	molecular_function	nitrogenase activity
C	0016491	molecular_function	oxidoreductase activity
C	0016612	cellular_component	molybdenum-iron nitrogenase complex
C	0046872	molecular_function	metal ion binding
C	0051536	molecular_function	iron-sulfur cluster binding
D	0000166	molecular_function	nucleotide binding
D	0005524	molecular_function	ATP binding
D	0009399	biological_process	nitrogen fixation
D	0016163	molecular_function	nitrogenase activity
D	0016491	molecular_function	oxidoreductase activity
D	0016612	cellular_component	molybdenum-iron nitrogenase complex
D	0046872	molecular_function	metal ion binding
D	0051536	molecular_function	iron-sulfur cluster binding
E	0000166	molecular_function	nucleotide binding
E	0005524	molecular_function	ATP binding
E	0009399	biological_process	nitrogen fixation
E	0016163	molecular_function	nitrogenase activity
E	0016491	molecular_function	oxidoreductase activity
E	0046872	molecular_function	metal ion binding
E	0051536	molecular_function	iron-sulfur cluster binding
E	0051539	molecular_function	4 iron, 4 sulfur cluster binding
F	0000166	molecular_function	nucleotide binding
F	0005524	molecular_function	ATP binding
F	0009399	biological_process	nitrogen fixation
F	0016163	molecular_function	nitrogenase activity
F	0016491	molecular_function	oxidoreductase activity
F	0046872	molecular_function	metal ion binding
F	0051536	molecular_function	iron-sulfur cluster binding
F	0051539	molecular_function	4 iron, 4 sulfur cluster binding
G	0000166	molecular_function	nucleotide binding
G	0005524	molecular_function	ATP binding
G	0009399	biological_process	nitrogen fixation
G	0016163	molecular_function	nitrogenase activity
G	0016491	molecular_function	oxidoreductase activity
G	0046872	molecular_function	metal ion binding
G	0051536	molecular_function	iron-sulfur cluster binding
G	0051539	molecular_function	4 iron, 4 sulfur cluster binding
H	0000166	molecular_function	nucleotide binding
H	0005524	molecular_function	ATP binding
H	0009399	biological_process	nitrogen fixation
H	0016163	molecular_function	nitrogenase activity
H	0016491	molecular_function	oxidoreductase activity
H	0046872	molecular_function	metal ion binding
H	0051536	molecular_function	iron-sulfur cluster binding
H	0051539	molecular_function	4 iron, 4 sulfur cluster binding
I	0000166	molecular_function	nucleotide binding
I	0005524	molecular_function	ATP binding
I	0009399	biological_process	nitrogen fixation
I	0016163	molecular_function	nitrogenase activity
I	0016491	molecular_function	oxidoreductase activity
I	0016612	cellular_component	molybdenum-iron nitrogenase complex
I	0046872	molecular_function	metal ion binding
I	0051536	molecular_function	iron-sulfur cluster binding
J	0000166	molecular_function	nucleotide binding
J	0005524	molecular_function	ATP binding
J	0009399	biological_process	nitrogen fixation
J	0016163	molecular_function	nitrogenase activity
J	0016491	molecular_function	oxidoreductase activity
J	0016612	cellular_component	molybdenum-iron nitrogenase complex
J	0046872	molecular_function	metal ion binding
J	0051536	molecular_function	iron-sulfur cluster binding
K	0000166	molecular_function	nucleotide binding
K	0005524	molecular_function	ATP binding
K	0009399	biological_process	nitrogen fixation
K	0016163	molecular_function	nitrogenase activity
K	0016491	molecular_function	oxidoreductase activity
K	0016612	cellular_component	molybdenum-iron nitrogenase complex
K	0046872	molecular_function	metal ion binding
K	0051536	molecular_function	iron-sulfur cluster binding
L	0000166	molecular_function	nucleotide binding
L	0005524	molecular_function	ATP binding
L	0009399	biological_process	nitrogen fixation
L	0016163	molecular_function	nitrogenase activity
L	0016491	molecular_function	oxidoreductase activity
L	0016612	cellular_component	molybdenum-iron nitrogenase complex
L	0046872	molecular_function	metal ion binding
L	0051536	molecular_function	iron-sulfur cluster binding
M	0000166	molecular_function	nucleotide binding
M	0005524	molecular_function	ATP binding
M	0009399	biological_process	nitrogen fixation
M	0016163	molecular_function	nitrogenase activity
M	0016491	molecular_function	oxidoreductase activity
M	0046872	molecular_function	metal ion binding
M	0051536	molecular_function	iron-sulfur cluster binding
M	0051539	molecular_function	4 iron, 4 sulfur cluster binding
N	0000166	molecular_function	nucleotide binding
N	0005524	molecular_function	ATP binding
N	0009399	biological_process	nitrogen fixation
N	0016163	molecular_function	nitrogenase activity
N	0016491	molecular_function	oxidoreductase activity
N	0046872	molecular_function	metal ion binding
N	0051536	molecular_function	iron-sulfur cluster binding
N	0051539	molecular_function	4 iron, 4 sulfur cluster binding
O	0000166	molecular_function	nucleotide binding
O	0005524	molecular_function	ATP binding
O	0009399	biological_process	nitrogen fixation
O	0016163	molecular_function	nitrogenase activity
O	0016491	molecular_function	oxidoreductase activity
O	0046872	molecular_function	metal ion binding
O	0051536	molecular_function	iron-sulfur cluster binding
O	0051539	molecular_function	4 iron, 4 sulfur cluster binding
P	0000166	molecular_function	nucleotide binding
P	0005524	molecular_function	ATP binding
P	0009399	biological_process	nitrogen fixation
P	0016163	molecular_function	nitrogenase activity
P	0016491	molecular_function	oxidoreductase activity
P	0046872	molecular_function	metal ion binding
P	0051536	molecular_function	iron-sulfur cluster binding
P	0051539	molecular_function	4 iron, 4 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA D 2099

Chain	Residue
B	ARG108
B	GLU109
D	ASP353
D	ASP357
D	HOH2469

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 2299

Chain	Residue
D	GLU109
B	ASP353
B	ASP357
B	HOH2477
D	ARG108

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG E 3092

Chain	Residue
E	SER16
E	ADP3091
E	ALF3093
E	HOH3131
E	HOH3132
E	HOH3133

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ALF E 3093

Chain	Residue
E	GLY11
E	GLY12
E	LYS15
E	ASP39
E	LYS41
E	LEU127
E	GLY128
E	ADP3091
E	MG3092
E	HOH3130
E	HOH3131
F	LYS10
F	GLY11

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG F 3192

Chain	Residue
F	SER16
F	ADP3191
F	ALF3193
F	HOH3196
F	HOH3197
F	HOH3198

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ALF F 3193

Chain	Residue
E	LYS10
E	GLY11
E	HOH3134
F	GLY11
F	GLY12
F	LYS15
F	ASP39
F	LYS41
F	GLY128
F	ADP3191
F	MG3192
F	HOH3196
F	HOH3197

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG G 3292

Chain	Residue
G	SER16
G	ADP3291
G	ALF3293
G	HOH3346
G	HOH3347
G	HOH3348

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ALF G 3293

Chain	Residue
G	GLY11
G	GLY12
G	LYS15
G	ASP39
G	LYS41
G	GLY128
G	ADP3291
G	MG3292
G	HOH3345
G	HOH3347
H	LYS10
H	GLY11

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG H 3392

Chain	Residue
H	SER16
H	ADP3391
H	ALF3393
H	HOH3417
H	HOH3418
H	HOH3419

site_id	BC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ALF H 3393

Chain	Residue
G	LYS10
G	GLY11
G	HOH3349
H	GLY11
H	GLY12
H	LYS15
H	ASP39
H	LYS41
H	GLY128
H	ADP3391
H	MG3392
H	HOH3418

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA L 4099

Chain	Residue
J	ARG108
J	GLU109
J	HOH4505
L	ASP353
L	ASP357

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA J 4299

Chain	Residue
J	ASP353
J	ASP357
J	HOH4506
L	ARG108
L	GLU109

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG M 5092

Chain	Residue
M	HOH5154
M	SER16
M	ADP5091
M	ALF5093
M	HOH5152
M	HOH5153

site_id	BC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ALF M 5093

Chain	Residue
M	GLY11
M	GLY12
M	LYS15
M	ASP39
M	LYS41
M	LEU127
M	GLY128
M	ADP5091
M	MG5092
M	HOH5151
M	HOH5152
M	HOH5153
N	LYS10
N	GLY11
N	HOH5202

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG N 5192

Chain	Residue
N	SER16
N	ADP5191
N	ALF5193
N	HOH5232
N	HOH5233
N	HOH5234

site_id	BC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ALF N 5193

Chain	Residue
M	LYS10
M	GLY11
M	HOH5102
M	HOH5155
N	GLY11
N	GLY12
N	LYS15
N	ASP39
N	LYS41
N	LEU127
N	GLY128
N	ADP5191
N	MG5192
N	HOH5232
N	HOH5233

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG O 5292

Chain	Residue
O	SER16
O	ADP5291
O	ALF5293
O	HOH5296
O	HOH5297
O	HOH5298

site_id	BC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ALF O 5293

Chain	Residue
O	GLY11
O	GLY12
O	LYS15
O	LYS41
O	LEU127
O	GLY128
O	ADP5291
O	MG5292
O	HOH5294
O	HOH5296
P	LYS10
P	GLY11

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG P 5392

Chain	Residue
P	SER16
P	ADP5391
P	ALF5393
P	HOH5396
P	HOH5397
P	HOH5398

site_id	CC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ALF P 5393

Chain	Residue
O	LYS10
O	GLY11
O	ASP129
O	HOH5394
P	GLY11
P	GLY12
P	LYS15
P	LYS41
P	GLY128
P	ADP5391
P	MG5392

site_id	CC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HCA A 2094

Chain	Residue
A	ALA65
A	GLY95
A	GLN191
A	GLY424
A	ILE425
A	LYS426
A	HIS442
A	CFM2096
A	HOH2097
A	HOH2106
A	HOH2113
A	HOH2131
A	HOH2132
A	HOH2138
A	HOH2224

site_id	CC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CFM A 2096

Chain	Residue
A	ARG96
A	HIS195
A	TYR229
A	ILE231
A	CYS275
A	ILE355
A	GLY356
A	GLY357
A	ARG359
A	PHE381
A	HIS442
A	HCA2094

site_id	CC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLF B 2098

Chain	Residue
A	CYS62
A	TYR64
A	VAL86
A	CYS88
A	TYR91
A	CYS154
A	GLY185
B	CYS70
B	PRO72
B	SER92
B	CYS95
B	TYR98
B	CYS153
B	SER188

site_id	CC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HCA C 2294

Chain	Residue
C	ARG96
C	GLN191
C	GLY424
C	ILE425
C	LYS426
C	HIS442
C	CFM2296
C	HOH2306
C	HOH2339
C	HOH2379
C	HOH2381
C	HOH2386
C	HOH2397
C	HOH2414

site_id	CC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CFM C 2296

Chain	Residue
C	ARG96
C	HIS195
C	TYR229
C	CYS275
C	SER278
C	GLY356
C	GLY357
C	LEU358
C	ARG359
C	PHE381
C	HIS442
C	HCA2294

site_id	CC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLF D 2298

Chain	Residue
C	CYS62
C	TYR64
C	PRO85
C	VAL86
C	CYS88
C	CYS154
C	GLY185
D	CYS70
D	PRO72
D	SER92
D	CYS95
D	TYR98
D	CYS153
D	SER188

site_id	CC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 E 3090

Chain	Residue
A	LEU158
B	VAL157
E	CYS97
E	ALA98
E	GLY99
E	CYS132
F	CYS97
F	ALA98
F	GLY99
F	CYS132

site_id	DC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ADP E 3091

Chain	Residue
E	GLY12
E	ILE13
E	GLY14
E	LYS15
E	SER16
E	THR17
E	ASN185
E	PRO212
E	ARG213
E	ASP214
E	VAL217
E	GLN218
E	GLU221
E	GLN236
E	MG3092
E	ALF3093
E	HOH3132
F	LYS10
F	GLU154
F	MET156

site_id	DC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ADP F 3191

Chain	Residue
E	LYS10
E	GLU154
E	MET156
F	GLY12
F	ILE13
F	GLY14
F	LYS15
F	SER16
F	THR17
F	ASN185
F	VAL211
F	PRO212
F	ARG213
F	ASP214
F	VAL217
F	GLN218
F	GLU221
F	GLN236
F	TYR240
F	HOH1505
F	MG3192
F	ALF3193
F	HOH3196
F	HOH3197

site_id	DC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SF4 G 3290

Chain	Residue
C	LEU158
D	VAL157
D	ILE158
G	CYS97
G	ALA98
G	GLY99
G	CYS132
H	CYS97
H	ALA98
H	GLY99
H	CYS132

site_id	DC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ADP G 3291

Chain	Residue
G	GLY12
G	ILE13
G	GLY14
G	LYS15
G	SER16
G	THR17
G	ASN185
G	VAL211
G	PRO212
G	ARG213
G	ASP214
G	GLN218
G	GLU221
G	GLN236
G	MG3292
G	ALF3293
G	HOH3346
G	HOH3347
H	LYS10
H	GLU154
H	MET156

site_id	DC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ADP H 3391

Chain	Residue
G	LYS10
G	GLU154
G	MET156
H	GLY12
H	ILE13
H	GLY14
H	LYS15
H	SER16
H	THR17
H	ASN185
H	PRO212
H	ARG213
H	ASP214
H	VAL217
H	GLN218
H	GLU221
H	GLN236
H	MG3392
H	ALF3393
H	HOH3402
H	HOH3417

site_id	DC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HCA I 4094

Chain	Residue
I	ALA65
I	ARG96
I	GLN191
I	GLY424
I	ILE425
I	LYS426
I	HIS442
I	CFM4096
I	HOH4107
I	HOH4109
I	HOH4147
I	HOH4150
I	HOH4194
I	HOH4204
I	HOH4225
I	HOH4286
J	HOH4361

site_id	DC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CFM I 4096

Chain	Residue
I	ARG96
I	HIS195
I	TYR229
I	CYS275
I	GLY356
I	GLY357
I	LEU358
I	ARG359
I	PHE381
I	HIS442
I	HCA4094

site_id	DC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLF J 4098

Chain	Residue
I	CYS62
I	TYR64
I	PRO85
I	VAL86
I	CYS88
I	CYS154
I	GLY185
J	CYS70
J	PRO72
J	SER92
J	CYS95
J	TYR98
J	CYS153
J	SER188

site_id	DC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HCA K 4294

Chain	Residue
K	ALA65
K	GLN191
K	ILE425
K	LYS426
K	HIS442
K	CFM4296
K	HOH4299
K	HOH4304
K	HOH4363
K	HOH4398
L	HOH4368

site_id	EC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CFM K 4296

Chain	Residue
K	ARG96
K	HIS195
K	TYR229
K	CYS275
K	GLY356
K	GLY357
K	LEU358
K	ARG359
K	PHE381
K	HIS442
K	HCA4294

site_id	EC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CLF L 4298

Chain	Residue
K	CYS62
K	TYR64
K	PRO85
K	VAL86
K	CYS88
K	TYR91
K	CYS154
K	GLY185
L	CYS70
L	PRO72
L	SER92
L	CYS95
L	TYR98
L	CYS153
L	SER188

site_id	EC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SF4 M 5090

Chain	Residue
I	LEU158
J	VAL157
M	CYS97
M	ALA98
M	GLY99
M	CYS132
N	CYS97
N	ALA98
N	GLY99
N	VAL131
N	CYS132

site_id	EC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ADP M 5091

Chain	Residue
M	GLY12
M	ILE13
M	GLY14
M	LYS15
M	SER16
M	THR17
M	ASN185
M	PRO212
M	ARG213
M	ASP214
M	GLN218
M	GLU221
M	GLN236
M	MG5092
M	ALF5093
M	HOH5113
M	HOH5152
M	HOH5153
N	LYS10
N	GLU154
N	MET156

site_id	EC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ADP N 5191

Chain	Residue
M	LYS10
M	GLU154
M	MET156
N	GLY12
N	ILE13
N	GLY14
N	LYS15
N	SER16
N	THR17
N	ASN185
N	PRO212
N	ARG213
N	ASP214
N	GLN218
N	GLU221
N	GLN236
N	MG5192
N	ALF5193
N	HOH5206
N	HOH5232
N	HOH5233

site_id	EC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 O 5290

Chain	Residue
K	LEU158
L	VAL157
O	CYS97
O	ALA98
O	GLY99
O	CYS132
P	CYS97
P	ALA98
P	GLY99
P	CYS132

site_id	EC7
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ADP O 5291

Chain	Residue
O	GLY12
O	ILE13
O	GLY14
O	LYS15
O	SER16
O	THR17
O	ASN185
O	PRO212
O	ARG213
O	ASP214
O	VAL217
O	GLN218
O	GLU221
O	GLN236
O	HOH1451
O	MG5292
O	ALF5293
O	HOH5296
P	LYS10
P	GLU154
P	MET155
P	MET156

site_id	EC8
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ADP P 5391

Chain	Residue
O	LYS10
O	GLU154
O	MET156
P	GLY12
P	ILE13
P	GLY14
P	LYS15
P	SER16
P	THR17
P	ASN185
P	VAL211
P	PRO212
P	ARG213
P	ASP214
P	VAL217
P	GLN218
P	GLU221
P	GLN236
P	TYR240
P	MG5392
P	ALF5393
P	HOH5396
P	HOH5397

Functional Information from PROSITE/UniProt

site_id	PS00090
Number of Residues	15
Details	NITROGENASE_1_2 Nitrogenases component 1 alpha and beta subunits signature 2. SECpigliGDDIeSV

Chain	Residue	Details
A	SER152-VAL166
B	THR151-PHE165

site_id	PS00692
Number of Residues	14
Details	NIFH_FRXC_2 NifH/frxC family signature 2. DvLGDVVCGGFAmP

Chain	Residue	Details
E	ASP125-PRO138

site_id	PS00699
Number of Residues	8
Details	NITROGENASE_1_1 Nitrogenases component 1 alpha and beta subunits signature 1. ISHGPVGC

Chain	Residue	Details
A	ILE81-CYS88
B	TYR88-CYS95

site_id	PS00746
Number of Residues	13
Details	NIFH_FRXC_1 NifH/frxC family signature 1. EsGGPepGvGCAG

Chain	Residue	Details
E	GLU87-GLY99

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	108
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Modified residue: {"description":"ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1f48

Chain	Residue	Details
E	LYS15
E	GLY12

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1f48

Chain	Residue	Details
F	LYS15
F	GLY12

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1f48

Chain	Residue	Details
G	LYS15
G	GLY12

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1f48

Chain	Residue	Details
H	LYS15
H	GLY12

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1f48

Chain	Residue	Details
M	LYS15
M	GLY12

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1f48

Chain	Residue	Details
N	LYS15
N	GLY12

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1f48

Chain	Residue	Details
O	LYS15
O	GLY12

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1f48

Chain	Residue	Details
P	LYS15
P	GLY12

site_id	MCSA1
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
E	LYS10	electrostatic stabiliser, hydrogen bond donor
E	LYS15	electrostatic stabiliser, hydrogen bond donor
E	LYS41	electrostatic stabiliser, hydrogen bond donor
E	ASP129	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
F	LYS10	electrostatic stabiliser, hydrogen bond donor
F	LYS15	electrostatic stabiliser, hydrogen bond donor
F	LYS41	electrostatic stabiliser, hydrogen bond donor
F	ASP129	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA3
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
G	LYS10	electrostatic stabiliser, hydrogen bond donor
G	LYS15	electrostatic stabiliser, hydrogen bond donor
G	LYS41	electrostatic stabiliser, hydrogen bond donor
G	ASP129	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA4
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
H	LYS10	electrostatic stabiliser, hydrogen bond donor
H	LYS15	electrostatic stabiliser, hydrogen bond donor
H	LYS41	electrostatic stabiliser, hydrogen bond donor
H	ASP129	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA5
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
M	LYS10	electrostatic stabiliser, hydrogen bond donor
M	LYS15	electrostatic stabiliser, hydrogen bond donor
M	LYS41	electrostatic stabiliser, hydrogen bond donor
M	ASP129	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA6
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
N	LYS10	electrostatic stabiliser, hydrogen bond donor
N	LYS15	electrostatic stabiliser, hydrogen bond donor
N	LYS41	electrostatic stabiliser, hydrogen bond donor
N	ASP129	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA7
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
O	LYS10	electrostatic stabiliser, hydrogen bond donor
O	LYS15	electrostatic stabiliser, hydrogen bond donor
O	LYS41	electrostatic stabiliser, hydrogen bond donor
O	ASP129	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA8
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
P	LYS10	electrostatic stabiliser, hydrogen bond donor
P	LYS15	electrostatic stabiliser, hydrogen bond donor
P	LYS41	electrostatic stabiliser, hydrogen bond donor
P	ASP129	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)