Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5L3S

Structure of the GTPase heterodimer of crenarchaeal SRP54 and FtsY

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003924	molecular_function	GTPase activity
A	0005525	molecular_function	GTP binding
A	0006614	biological_process	SRP-dependent cotranslational protein targeting to membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0048500	cellular_component	signal recognition particle
B	0005525	molecular_function	GTP binding
B	0006614	biological_process	SRP-dependent cotranslational protein targeting to membrane
B	0016887	molecular_function	ATP hydrolysis activity
C	0003924	molecular_function	GTPase activity
C	0005525	molecular_function	GTP binding
C	0006614	biological_process	SRP-dependent cotranslational protein targeting to membrane
C	0016887	molecular_function	ATP hydrolysis activity
C	0048500	cellular_component	signal recognition particle
D	0005525	molecular_function	GTP binding
D	0006614	biological_process	SRP-dependent cotranslational protein targeting to membrane
D	0016887	molecular_function	ATP hydrolysis activity
E	0003924	molecular_function	GTPase activity
E	0005525	molecular_function	GTP binding
E	0006614	biological_process	SRP-dependent cotranslational protein targeting to membrane
E	0016887	molecular_function	ATP hydrolysis activity
E	0048500	cellular_component	signal recognition particle
F	0005525	molecular_function	GTP binding
F	0006614	biological_process	SRP-dependent cotranslational protein targeting to membrane
F	0016887	molecular_function	ATP hydrolysis activity
G	0003924	molecular_function	GTPase activity
G	0005525	molecular_function	GTP binding
G	0006614	biological_process	SRP-dependent cotranslational protein targeting to membrane
G	0016887	molecular_function	ATP hydrolysis activity
G	0048500	cellular_component	signal recognition particle
H	0005525	molecular_function	GTP binding
H	0006614	biological_process	SRP-dependent cotranslational protein targeting to membrane
H	0016887	molecular_function	ATP hydrolysis activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	28
Details	binding site for residue GNP A 301

Chain	Residue
A	GLN105
A	GLN142
A	GLY188
A	LYS246
A	ASP248
A	GLY271
A	THR272
A	GLY273
A	GLU274
A	MG302
A	HOH429
A	GLY106
A	HOH439
A	HOH443
A	HOH453
A	HOH472
A	HOH477
A	HOH489
B	ASN182
B	ARG213
B	GNP401
A	SER107
A	GLY108
A	LYS109
A	THR110
A	THR111
A	LYS115
A	ARG136

site_id	AC2
Number of Residues	5
Details	binding site for residue MG A 302

Chain	Residue
A	THR110
A	GNP301
A	HOH429
A	HOH439
A	HOH472

site_id	AC3
Number of Residues	12
Details	binding site for residue G A 303

Chain	Residue
A	VAL134
A	TYR135
A	ARG136
A	PRO137
A	ALA138
A	ALA139
A	TYR140
A	ASP141
A	PRO158
A	GLN161
A	HOH408
B	TYR222

site_id	AC4
Number of Residues	2
Details	binding site for residue GOL A 304

Chain	Residue
A	ASN40
A	SER46

site_id	AC5
Number of Residues	6
Details	binding site for residue GOL A 305

Chain	Residue
A	ILE270
A	ASN283
A	ARG286
A	ARG290
A	HOH403
A	HOH441

site_id	AC6
Number of Residues	7
Details	binding site for residue GOL A 306

Chain	Residue
A	LEU146
A	GLN149
A	ILE276
A	HOH402
B	PHE212
B	ALA214
B	HOH637

site_id	AC7
Number of Residues	3
Details	binding site for residue SO4 A 307

Chain	Residue
A	TYR192
A	GLY193
A	ARG232

site_id	AC8
Number of Residues	5
Details	binding site for residue SO4 A 308

Chain	Residue
A	TYR192
A	LYS225
A	ASP228
A	ARG232
A	HOH450

site_id	AC9
Number of Residues	7
Details	binding site for residue SO4 A 309

Chain	Residue
A	TYR140
A	ASP141
A	PRO158
A	HOH408
G	TYR140
G	ASP141
G	HOH433

site_id	AD1
Number of Residues	30
Details	binding site for residue GNP B 401

Chain	Residue
B	HOH527
B	HOH532
B	HOH545
B	HOH547
B	HOH553
B	HOH555
A	GLN105
A	ARG136
A	HIS190
A	GLU195
A	GNP301
A	HOH489
B	ASN182
B	GLY183
B	VAL184
B	GLY185
B	LYS186
B	THR187
B	THR188
B	LYS192
B	ARG213
B	GLN219
B	GLY265
B	LYS321
B	ASP323
B	GLY346
B	VAL347
B	GLY348
B	GLN349
B	MG402

site_id	AD2
Number of Residues	5
Details	binding site for residue MG B 402

Chain	Residue
B	THR187
B	GNP401
B	HOH527
B	HOH532
B	HOH547

site_id	AD3
Number of Residues	4
Details	binding site for residue GOL B 403

Chain	Residue
A	TYR135
B	ASN350
B	TYR351
B	HOH550

site_id	AD4
Number of Residues	8
Details	binding site for residue GOL B 404

Chain	Residue
A	HOH419
B	THR211
B	PHE212
B	ARG213
B	ALA215
B	ALA216
B	GLN217
B	GLU218

site_id	AD5
Number of Residues	9
Details	binding site for residue GOL B 405

Chain	Residue
B	LYS172
B	ASN201
B	SER203
B	ASP257
B	HOH522
B	HOH620
C	PRO92
C	LEU95
C	HOH477

site_id	AD6
Number of Residues	4
Details	binding site for residue GOL B 406

Chain	Residue
B	LYS278
B	ARG289
B	VAL312
B	SO4408

site_id	AD7
Number of Residues	4
Details	binding site for residue SO4 B 407

Chain	Residue
B	LEU231
B	ILE232
B	ARG233
B	GLY234

site_id	AD8
Number of Residues	3
Details	binding site for residue SO4 B 408

Chain	Residue
B	ARG282
B	GOL406
B	HOH612

site_id	AD9
Number of Residues	27
Details	binding site for residue GNP C 301

Chain	Residue
C	GLN105
C	GLY106
C	SER107
C	GLY108
C	LYS109
C	THR110
C	THR111
C	LYS115
C	ARG136
C	GLN142
C	GLY188
C	LYS246
C	ASP248
C	GLY271
C	THR272
C	GLY273
C	GLU274
C	MG302
C	HOH431
C	HOH447
C	HOH456
C	HOH473
C	HOH490
D	ASN182
D	ARG213
D	GNP401
D	HOH542

site_id	AE1
Number of Residues	5
Details	binding site for residue MG C 302

Chain	Residue
C	THR110
C	GNP301
C	HOH447
C	HOH452
C	HOH456

site_id	AE2
Number of Residues	15
Details	binding site for residue G C 303

Chain	Residue
C	VAL134
C	TYR135
C	ARG136
C	PRO137
C	ALA138
C	ALA139
C	TYR140
C	ASP141
C	PRO158
C	GLN161
C	HOH413
C	HOH459
C	HOH467
C	HOH501
D	TYR222

site_id	AE3
Number of Residues	7
Details	binding site for residue GOL C 304

Chain	Residue
C	ILE270
C	PHE282
C	ASN283
C	ARG286
C	ARG290
C	HOH401
C	HOH412

site_id	AE4
Number of Residues	7
Details	binding site for residue GOL C 305

Chain	Residue
C	GLN149
C	GLU274
C	LYS275
C	HOH411
D	PHE212
D	HOH528
D	HOH607

site_id	AE5
Number of Residues	3
Details	binding site for residue SO4 C 306

Chain	Residue
C	THR196
C	ARG232
C	HOH417

site_id	AE6
Number of Residues	30
Details	binding site for residue GNP D 401

Chain	Residue
C	GLN105
C	ARG136
C	HIS190
C	GLU195
C	GNP301
D	ASN182
D	GLY183
D	VAL184
D	GLY185
D	LYS186
D	THR187
D	THR188
D	LYS192
D	ARG213
D	GLN219
D	GLY265
D	LYS321
D	ASP323
D	GLY346
D	VAL347
D	GLY348
D	GLN349
D	MG402
D	HOH512
D	HOH514
D	HOH516
D	HOH535
D	HOH542
D	HOH560
D	HOH580

site_id	AE7
Number of Residues	5
Details	binding site for residue MG D 402

Chain	Residue
D	THR187
D	GNP401
D	HOH512
D	HOH516
D	HOH580

site_id	AE8
Number of Residues	4
Details	binding site for residue GOL D 403

Chain	Residue
D	GLN349
D	ASN350
D	TYR351
D	HOH556

site_id	AE9
Number of Residues	28
Details	binding site for residue GNP E 301

Chain	Residue
E	GLN105
E	GLY106
E	SER107
E	GLY108
E	LYS109
E	THR110
E	THR111
E	LYS115
E	ARG136
E	GLN142
E	GLY188
E	LYS246
E	ASP248
E	GLY271
E	THR272
E	GLY273
E	GLU274
E	MG302
E	HOH420
E	HOH421
E	HOH432
E	HOH435
E	HOH444
E	HOH470
E	HOH471
F	ASN182
F	MET267
F	GNP401

site_id	AF1
Number of Residues	5
Details	binding site for residue MG E 302

Chain	Residue
E	THR110
E	GNP301
E	HOH421
E	HOH432
E	HOH435

site_id	AF2
Number of Residues	15
Details	binding site for residue G E 303

Chain	Residue
E	VAL134
E	TYR135
E	ARG136
E	PRO137
E	ALA138
E	ALA139
E	TYR140
E	PRO158
E	GLN161
E	HOH415
E	HOH422
E	HOH476
E	HOH518
F	TYR222
F	LYS226

site_id	AF3
Number of Residues	3
Details	binding site for residue GOL E 304

Chain	Residue
E	PHE282
E	ASN283
E	ARG290

site_id	AF4
Number of Residues	10
Details	binding site for residue GOL E 305

Chain	Residue
E	LEU146
E	GLN149
E	GLU274
E	LYS275
E	ILE276
E	HOH401
E	HOH486
E	HOH500
F	PHE212
F	ALA214

site_id	AF5
Number of Residues	5
Details	binding site for residue SO4 E 306

Chain	Residue
E	TYR192
E	GLY193
E	ARG232
E	HOH418
F	ASP325

site_id	AF6
Number of Residues	30
Details	binding site for residue GNP F 401

Chain	Residue
E	GLN105
E	ARG136
E	HIS190
E	GLU195
E	GNP301
E	HOH470
F	ASN182
F	GLY183
F	VAL184
F	GLY185
F	LYS186
F	THR187
F	THR188
F	LYS192
F	ARG213
F	GLN219
F	GLY265
F	LYS321
F	ASP323
F	GLY346
F	VAL347
F	GLY348
F	GLN349
F	MG402
F	HOH522
F	HOH523
F	HOH528
F	HOH536
F	HOH551
F	HOH555

site_id	AF7
Number of Residues	5
Details	binding site for residue MG F 402

Chain	Residue
F	THR187
F	GNP401
F	HOH523
F	HOH528
F	HOH536

site_id	AF8
Number of Residues	5
Details	binding site for residue GOL F 403

Chain	Residue
E	TYR135
F	GLN349
F	ASN350
F	TYR351
F	HOH525

site_id	AF9
Number of Residues	28
Details	binding site for residue GNP G 301

Chain	Residue
G	GLN105
G	GLY106
G	SER107
G	GLY108
G	LYS109
G	THR110
G	THR111
G	LYS115
G	ARG136
G	GLN142
G	GLY188
G	LYS246
G	ASP248
G	GLY271
G	THR272
G	GLY273
G	GLU274
G	MG302
G	HOH424
G	HOH430
G	HOH440
G	HOH456
G	HOH489
G	HOH494
H	ASN182
H	ARG213
H	GNP401
H	HOH558

site_id	AG1
Number of Residues	5
Details	binding site for residue MG G 302

Chain	Residue
G	THR110
G	GNP301
G	HOH430
G	HOH440
G	HOH456

site_id	AG2
Number of Residues	14
Details	binding site for residue G G 303

Chain	Residue
G	VAL134
G	TYR135
G	PRO137
G	ALA138
G	ALA139
G	TYR140
G	ASP141
G	PRO158
G	GLN161
G	HOH423
G	HOH433
G	HOH523
H	TYR222
H	LYS226

site_id	AG3
Number of Residues	7
Details	binding site for residue GOL G 304

Chain	Residue
A	ASN177
G	TYR125
G	LYS126
G	VAL127
G	GLY151
G	VAL152
G	HOH410

site_id	AG4
Number of Residues	8
Details	binding site for residue GOL G 305

Chain	Residue
G	LEU146
G	GLN149
G	GLU274
G	LYS275
G	ILE276
H	PHE212
H	TYR236
H	HOH605

site_id	AG5
Number of Residues	8
Details	binding site for residue GOL G 306

Chain	Residue
G	MET247
G	PHE282
G	ASN283
G	ARG286
G	PHE287
G	ARG290
G	HOH403
G	HOH438

site_id	AG6
Number of Residues	5
Details	binding site for residue SO4 G 307

Chain	Residue
G	TYR192
G	GLY193
G	THR196
G	ARG232
H	ASP325

site_id	AG7
Number of Residues	30
Details	binding site for residue GNP H 401

Chain	Residue
G	GLN105
G	ARG136
G	HIS190
G	GLU195
G	GNP301
H	ASN182
H	GLY183
H	VAL184
H	GLY185
H	LYS186
H	THR187
H	THR188
H	LYS192
H	ARG213
H	GLN219
H	GLY265
H	LYS321
H	ASP323
H	GLY346
H	VAL347
H	GLY348
H	GLN349
H	MG402
H	HOH524
H	HOH533
H	HOH546
H	HOH547
H	HOH549
H	HOH558
H	HOH571

site_id	AG8
Number of Residues	5
Details	binding site for residue MG H 402

Chain	Residue
H	THR187
H	GNP401
H	HOH533
H	HOH549
H	HOH571

site_id	AG9
Number of Residues	5
Details	binding site for residue GOL H 403

Chain	Residue
H	GLN349
H	ASN350
H	TYR351
H	HOH506
H	HOH541

site_id	AH1
Number of Residues	2
Details	binding site for residue GOL H 404

Chain	Residue
H	ARG289
H	SO4405

site_id	AH2
Number of Residues	5
Details	binding site for residue SO4 H 405

Chain	Residue
H	LYS278
H	ARG282
H	GOL404
H	HOH525
H	HOH529

Functional Information from PROSITE/UniProt

site_id	PS00300
Number of Residues	14
Details	SRP54 SRP54-type proteins GTP-binding domain signature. PVvYMGVGQnYddL

Chain	Residue	Details
B	PRO341-LEU354

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00920

Chain	Residue	Details
B	GLY180
H	GLY180
H	ASP262
H	THR320
B	ASP262
B	THR320
D	GLY180
D	ASP262
D	THR320
F	GLY180
F	ASP262
F	THR320

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