Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1LGR

INTERACTIONS OF NUCLEOTIDES WITH FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004356	molecular_function	glutamine synthetase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006542	biological_process	glutamine biosynthetic process
A	0016020	cellular_component	membrane
A	0016874	molecular_function	ligase activity
A	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
A	0019740	biological_process	nitrogen utilization
A	0030145	molecular_function	manganese ion binding
A	0046872	molecular_function	metal ion binding
A	0051260	biological_process	protein homooligomerization
B	0003824	molecular_function	catalytic activity
B	0004356	molecular_function	glutamine synthetase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006542	biological_process	glutamine biosynthetic process
B	0016020	cellular_component	membrane
B	0016874	molecular_function	ligase activity
B	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
B	0019740	biological_process	nitrogen utilization
B	0030145	molecular_function	manganese ion binding
B	0046872	molecular_function	metal ion binding
B	0051260	biological_process	protein homooligomerization
C	0003824	molecular_function	catalytic activity
C	0004356	molecular_function	glutamine synthetase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006542	biological_process	glutamine biosynthetic process
C	0016020	cellular_component	membrane
C	0016874	molecular_function	ligase activity
C	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
C	0019740	biological_process	nitrogen utilization
C	0030145	molecular_function	manganese ion binding
C	0046872	molecular_function	metal ion binding
C	0051260	biological_process	protein homooligomerization
D	0003824	molecular_function	catalytic activity
D	0004356	molecular_function	glutamine synthetase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006542	biological_process	glutamine biosynthetic process
D	0016020	cellular_component	membrane
D	0016874	molecular_function	ligase activity
D	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
D	0019740	biological_process	nitrogen utilization
D	0030145	molecular_function	manganese ion binding
D	0046872	molecular_function	metal ion binding
D	0051260	biological_process	protein homooligomerization
E	0003824	molecular_function	catalytic activity
E	0004356	molecular_function	glutamine synthetase activity
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0006542	biological_process	glutamine biosynthetic process
E	0016020	cellular_component	membrane
E	0016874	molecular_function	ligase activity
E	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
E	0019740	biological_process	nitrogen utilization
E	0030145	molecular_function	manganese ion binding
E	0046872	molecular_function	metal ion binding
E	0051260	biological_process	protein homooligomerization
F	0003824	molecular_function	catalytic activity
F	0004356	molecular_function	glutamine synthetase activity
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0006542	biological_process	glutamine biosynthetic process
F	0016020	cellular_component	membrane
F	0016874	molecular_function	ligase activity
F	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
F	0019740	biological_process	nitrogen utilization
F	0030145	molecular_function	manganese ion binding
F	0046872	molecular_function	metal ion binding
F	0051260	biological_process	protein homooligomerization
G	0003824	molecular_function	catalytic activity
G	0004356	molecular_function	glutamine synthetase activity
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0006542	biological_process	glutamine biosynthetic process
G	0016020	cellular_component	membrane
G	0016874	molecular_function	ligase activity
G	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
G	0019740	biological_process	nitrogen utilization
G	0030145	molecular_function	manganese ion binding
G	0046872	molecular_function	metal ion binding
G	0051260	biological_process	protein homooligomerization
H	0003824	molecular_function	catalytic activity
H	0004356	molecular_function	glutamine synthetase activity
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0006542	biological_process	glutamine biosynthetic process
H	0016020	cellular_component	membrane
H	0016874	molecular_function	ligase activity
H	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
H	0019740	biological_process	nitrogen utilization
H	0030145	molecular_function	manganese ion binding
H	0046872	molecular_function	metal ion binding
H	0051260	biological_process	protein homooligomerization
I	0003824	molecular_function	catalytic activity
I	0004356	molecular_function	glutamine synthetase activity
I	0005524	molecular_function	ATP binding
I	0005737	cellular_component	cytoplasm
I	0006542	biological_process	glutamine biosynthetic process
I	0016020	cellular_component	membrane
I	0016874	molecular_function	ligase activity
I	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
I	0019740	biological_process	nitrogen utilization
I	0030145	molecular_function	manganese ion binding
I	0046872	molecular_function	metal ion binding
I	0051260	biological_process	protein homooligomerization
J	0003824	molecular_function	catalytic activity
J	0004356	molecular_function	glutamine synthetase activity
J	0005524	molecular_function	ATP binding
J	0005737	cellular_component	cytoplasm
J	0006542	biological_process	glutamine biosynthetic process
J	0016020	cellular_component	membrane
J	0016874	molecular_function	ligase activity
J	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
J	0019740	biological_process	nitrogen utilization
J	0030145	molecular_function	manganese ion binding
J	0046872	molecular_function	metal ion binding
J	0051260	biological_process	protein homooligomerization
K	0003824	molecular_function	catalytic activity
K	0004356	molecular_function	glutamine synthetase activity
K	0005524	molecular_function	ATP binding
K	0005737	cellular_component	cytoplasm
K	0006542	biological_process	glutamine biosynthetic process
K	0016020	cellular_component	membrane
K	0016874	molecular_function	ligase activity
K	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
K	0019740	biological_process	nitrogen utilization
K	0030145	molecular_function	manganese ion binding
K	0046872	molecular_function	metal ion binding
K	0051260	biological_process	protein homooligomerization
L	0003824	molecular_function	catalytic activity
L	0004356	molecular_function	glutamine synthetase activity
L	0005524	molecular_function	ATP binding
L	0005737	cellular_component	cytoplasm
L	0006542	biological_process	glutamine biosynthetic process
L	0016020	cellular_component	membrane
L	0016874	molecular_function	ligase activity
L	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
L	0019740	biological_process	nitrogen utilization
L	0030145	molecular_function	manganese ion binding
L	0046872	molecular_function	metal ion binding
L	0051260	biological_process	protein homooligomerization

Functional Information from PDB Data

site_id	A
Number of Residues	14
Details	CATALYTIC SITE IN CHAIN A

Chain	Residue
A	GLU129
A	ARG359
A	ASP50
A	AMP471
A	MN469
A	MN470
A	GLU131
A	HIS269
A	GLU212
A	GLU220
A	GLU357
A	ARG321
A	GLY265
A	ARG339

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN A 469

Chain	Residue
A	GLU131
A	GLU212
A	GLU220

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN A 470

Chain	Residue
A	GLU129
A	HIS269
A	GLU357

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN B 483

Chain	Residue
B	GLU131
B	GLU212
B	GLU220

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN B 484

Chain	Residue
B	GLU129
B	HIS269
B	GLU357

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN C 485

Chain	Residue
C	GLU131
C	GLU212
C	GLU220

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN C 486

Chain	Residue
C	GLU129
C	HIS269
C	GLU357

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN D 487

Chain	Residue
D	GLU131
D	GLU212
D	GLU220

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN D 488

Chain	Residue
D	GLU129
D	HIS269
D	GLU357

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN E 489

Chain	Residue
E	GLU131
E	GLU212
E	GLU220

site_id	B
Number of Residues	14
Details	CATALYTIC SITE IN CHAIN B

Chain	Residue
B	GLU129
B	GLU131
B	HIS269
B	GLU212
B	GLU220
B	GLU357
B	ARG321
B	GLY265
B	ARG339
B	ARG359
B	ASP50
B	AMP472
B	MN483
B	MN484

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN E 490

Chain	Residue
E	GLU129
E	HIS269
E	GLU357

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN F 491

Chain	Residue
F	GLU131
F	GLU212
F	GLU220

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN F 492

Chain	Residue
F	GLU129
F	HIS269
F	GLU357

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN G 493

Chain	Residue
G	GLU131
G	GLU212
G	GLU220

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN G 494

Chain	Residue
G	GLU129
G	HIS269
G	GLU357

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN H 495

Chain	Residue
H	GLU131
H	GLU212
H	GLU220

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN H 496

Chain	Residue
H	GLU129
H	HIS269
H	GLU357

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN I 497

Chain	Residue
I	GLU131
I	GLU212
I	GLU220

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN I 498

Chain	Residue
I	GLU129
I	HIS269
I	GLU357

site_id	C
Number of Residues	14
Details	CATALYTIC SITE IN CHAIN C

Chain	Residue
C	GLU129
C	GLU131
C	HIS269
C	GLU212
C	GLU220
C	GLU357
C	ARG321
C	GLY265
C	ARG339
C	ARG359
C	ASP50
C	AMP473
C	MN485
C	MN486

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN J 499

Chain	Residue
J	GLU131
J	GLU212
J	GLU220

site_id	CC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN J 500

Chain	Residue
J	GLU129
J	HIS269
J	GLU357

site_id	CC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN K 501

Chain	Residue
K	GLU131
K	GLU212
K	GLU220

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN K 502

Chain	Residue
K	GLU129
K	HIS269
K	GLU357

site_id	CC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN L 503

Chain	Residue
L	GLU131
L	GLU212
L	GLU220

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN L 504

Chain	Residue
L	GLU129
L	HIS269
L	GLU357

site_id	CC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AMP A 471

Chain	Residue
A	LEU125
A	GLY127
A	GLU207
A	THR223
A	PHE225
A	HIS271
A	SER273
A	ARG355

site_id	CC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AMP B 472

Chain	Residue
B	LEU125
B	GLY127
B	GLU207
B	THR223
B	PHE225
B	HIS271
B	SER273
B	ARG355

site_id	CC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AMP C 473

Chain	Residue
C	LEU125
C	GLY127
C	GLU207
C	THR223
C	PHE225
C	HIS271
C	SER273
C	ARG355

site_id	D
Number of Residues	14
Details	CATALYTIC SITE IN CHAIN D

Chain	Residue
D	GLU129
D	GLU131
D	HIS269
D	GLU212
D	GLU220
D	GLU357
D	ARG321
D	GLY265
D	ARG339
D	ARG359
D	ASP50
D	AMP474
D	MN487
D	MN488

site_id	DC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AMP D 474

Chain	Residue
D	LEU125
D	GLY127
D	GLU207
D	THR223
D	PHE225
D	HIS271
D	SER273
D	ARG355

site_id	DC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AMP E 475

Chain	Residue
E	LEU125
E	GLY127
E	GLU207
E	THR223
E	PHE225
E	HIS271
E	SER273
E	ARG355

site_id	DC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AMP F 476

Chain	Residue
F	LEU125
F	GLY127
F	GLU207
F	THR223
F	PHE225
F	HIS271
F	SER273
F	ARG355

site_id	DC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AMP G 477

Chain	Residue
G	LEU125
G	GLY127
G	GLU207
G	THR223
G	PHE225
G	HIS271
G	SER273
G	ARG355

site_id	DC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AMP H 478

Chain	Residue
H	LEU125
H	GLY127
H	GLU207
H	THR223
H	PHE225
H	HIS271
H	SER273
H	ARG355

site_id	DC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AMP I 479

Chain	Residue
I	LEU125
I	GLY127
I	GLU207
I	THR223
I	PHE225
I	HIS271
I	SER273
I	ARG355

site_id	DC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AMP J 480

Chain	Residue
J	LEU125
J	GLY127
J	GLU207
J	THR223
J	PHE225
J	HIS271
J	SER273
J	ARG355

site_id	DC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AMP K 481

Chain	Residue
K	LEU125
K	GLY127
K	GLU207
K	THR223
K	PHE225
K	HIS271
K	SER273
K	ARG355

site_id	DC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AMP L 482

Chain	Residue
L	LEU125
L	GLY127
L	GLU207
L	THR223
L	PHE225
L	HIS271
L	SER273
L	ARG355

site_id	E
Number of Residues	14
Details	CATALYTIC SITE IN CHAIN E

Chain	Residue
E	GLU129
E	GLU131
E	HIS269
E	GLU212
E	GLU220
E	GLU357
E	ARG321
E	GLY265
E	ARG339
E	ARG359
E	ASP50
E	AMP475
E	MN489
E	MN490

site_id	F
Number of Residues	14
Details	CATALYTIC SITE IN CHAIN F

Chain	Residue
F	GLU129
F	GLU131
F	HIS269
F	GLU212
F	GLU220
F	GLU357
F	ARG321
F	GLY265
F	ARG339
F	ARG359
F	ASP50
F	AMP476
F	MN491
F	MN492

site_id	G
Number of Residues	14
Details	CATALYTIC SITE IN CHAIN G

Chain	Residue
G	GLU129
G	GLU131
G	HIS269
G	GLU212
G	GLU220
G	GLU357
G	ARG321
G	GLY265
G	ARG339
G	ARG359
G	ASP50
G	AMP477
G	MN493
G	MN494

site_id	H
Number of Residues	14
Details	CATALYTIC SITE IN CHAIN H

Chain	Residue
H	GLU131
H	HIS269
H	GLU212
H	GLU220
H	GLU357
H	ARG321
H	GLY265
H	ARG339
H	ARG359
H	ASP50
H	AMP478
H	MN495
H	MN496
H	GLU129

site_id	I
Number of Residues	14
Details	CATALYTIC SITE IN CHAIN I

Chain	Residue
I	GLU129
I	GLU131
I	HIS269
I	GLU212
I	GLU220
I	GLU357
I	ARG321
I	GLY265
I	ARG339
I	ARG359
I	ASP50
I	AMP479
I	MN497
I	MN498

site_id	J
Number of Residues	14
Details	CATALYTIC SITE IN CHAIN J

Chain	Residue
J	GLU129
J	GLU131
J	HIS269
J	GLU212
J	GLU220
J	GLU357
J	ARG321
J	GLY265
J	ARG339
J	ARG359
J	ASP50
J	AMP480
J	MN499
J	MN500

site_id	K
Number of Residues	14
Details	CATALYTIC SITE IN CHAIN K

Chain	Residue
K	GLU129
K	GLU131
K	HIS269
K	GLU212
K	GLU220
K	GLU357
K	ARG321
K	GLY265
K	ARG339
K	ARG359
K	ASP50
K	AMP481
K	MN501
K	MN502

site_id	L
Number of Residues	14
Details	CATALYTIC SITE IN CHAIN L

Chain	Residue
L	GLU129
L	GLU131
L	HIS269
L	GLU212
L	GLU220
L	GLU357
L	ARG321
L	GLY265
L	ARG339
L	ARG359
L	ASP50
L	AMP482
L	MN503
L	MN504

Functional Information from PROSITE/UniProt

site_id	PS00180
Number of Residues	19
Details	GLNA_1 Glutamine synthetase signature 1. FDGSSiggwkginESDmvL

Chain	Residue	Details
A	PHE49-LEU67

site_id	PS00181
Number of Residues	16
Details	GLNA_ATP Glutamine synthetase putative ATP-binding region signature. KPMfgd..NGSGmHchmS

Chain	Residue	Details
A	LYS258-SER273

site_id	PS00182
Number of Residues	13
Details	GLNA_ADENYLATION Glutamine synthetase class-I adenylation site. KIhpgepMDKNLY

Chain	Residue	Details
A	LYS385-TYR397

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:11329256, ECO:0000269\|PubMed:2572586, ECO:0000269\|PubMed:8099447, ECO:0007744\|PDB:1F1H, ECO:0007744\|PDB:1F52, ECO:0007744\|PDB:1FPY, ECO:0007744\|PDB:2GLS, ECO:0007744\|PDB:2LGS

Chain	Residue	Details
A	PRO130
E	CYS270
F	PRO130
F	CYS270
G	PRO130
G	CYS270
H	PRO130
H	CYS270
I	PRO130
I	CYS270
J	PRO130
A	CYS270
J	CYS270
K	PRO130
K	CYS270
L	PRO130
L	CYS270
B	PRO130
B	CYS270
C	PRO130
C	CYS270
D	PRO130
D	CYS270
E	PRO130

site_id	SWS_FT_FI2
Number of Residues	36
Details	BINDING: BINDING => ECO:0000269\|PubMed:11329256, ECO:0000269\|PubMed:7727369, ECO:0000269\|PubMed:8099447, ECO:0007744\|PDB:1F1H, ECO:0007744\|PDB:1F52, ECO:0007744\|PDB:1FPY, ECO:0007744\|PDB:1LGR, ECO:0007744\|PDB:2LGS

Chain	Residue	Details
A	PHE132
D	PHE132
D	VAL213
D	VAL221
E	PHE132
E	VAL213
E	VAL221
F	PHE132
F	VAL213
F	VAL221
G	PHE132
A	VAL213
G	VAL213
G	VAL221
H	PHE132
H	VAL213
H	VAL221
I	PHE132
I	VAL213
I	VAL221
J	PHE132
J	VAL213
A	VAL221
J	VAL221
K	PHE132
K	VAL213
K	VAL221
L	PHE132
L	VAL213
L	VAL221
B	PHE132
B	VAL213
B	VAL221
C	PHE132
C	VAL213
C	VAL221

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:7727369, ECO:0007744\|PDB:1LGR

Chain	Residue	Details
A	ALA208
J	ALA208
K	ALA208
L	ALA208
B	ALA208
C	ALA208
D	ALA208
E	ALA208
F	ALA208
G	ALA208
H	ALA208
I	ALA208

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:7727369, ECO:0000269\|PubMed:8099447, ECO:0000305\|PubMed:11329256, ECO:0007744\|PDB:1F1H, ECO:0007744\|PDB:1FPY, ECO:0007744\|PDB:1LGR, ECO:0007744\|PDB:2LGS

Chain	Residue	Details
A	GLY265
J	GLY265
K	GLY265
L	GLY265
B	GLY265
C	GLY265
D	GLY265
E	GLY265
F	GLY265
G	GLY265
H	GLY265
I	GLY265

site_id	SWS_FT_FI5
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P12425

Chain	Residue	Details
A	SER266
J	SER266
K	SER266
L	SER266
B	SER266
C	SER266
D	SER266
E	SER266
F	SER266
G	SER266
H	SER266
I	SER266

site_id	SWS_FT_FI6
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:11329256, ECO:0007744\|PDB:1F1H, ECO:0007744\|PDB:1F52, ECO:0007744\|PDB:1FPY

Chain	Residue	Details
A	MET272
J	MET272
K	MET272
L	MET272
B	MET272
C	MET272
D	MET272
E	MET272
F	MET272
G	MET272
H	MET272
I	MET272

site_id	SWS_FT_FI7
Number of Residues	24
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P77961

Chain	Residue	Details
A	LEU274
E	ALA353
F	LEU274
F	ALA353
G	LEU274
G	ALA353
H	LEU274
H	ALA353
I	LEU274
I	ALA353
J	LEU274
A	ALA353
J	ALA353
K	LEU274
K	ALA353
L	LEU274
L	ALA353
B	LEU274
B	ALA353
C	LEU274
C	ALA353
D	LEU274
D	ALA353
E	LEU274

site_id	SWS_FT_FI8
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:8099447, ECO:0000305\|PubMed:11329256, ECO:0007744\|PDB:1FPY, ECO:0007744\|PDB:2LGS

Chain	Residue	Details
A	LEU322
J	LEU322
K	LEU322
L	LEU322
B	LEU322
C	LEU322
D	LEU322
E	LEU322
F	LEU322
G	LEU322
H	LEU322
I	LEU322

site_id	SWS_FT_FI9
Number of Residues	12
Details	BINDING: BINDING => ECO:0000305\|PubMed:11329256, ECO:0007744\|PDB:1FPY

Chain	Residue	Details
A	ALA328
J	ALA328
K	ALA328
L	ALA328
B	ALA328
C	ALA328
D	ALA328
E	ALA328
F	ALA328
G	ALA328
H	ALA328
I	ALA328

site_id	SWS_FT_FI10
Number of Residues	24
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P9WN39

Chain	Residue	Details
A	SER340
E	ILE345
F	SER340
F	ILE345
G	SER340
G	ILE345
H	SER340
H	ILE345
I	SER340
I	ILE345
J	SER340
A	ILE345
J	ILE345
K	SER340
K	ILE345
L	SER340
L	ILE345
B	SER340
B	ILE345
C	SER340
C	ILE345
D	SER340
D	ILE345
E	SER340

site_id	SWS_FT_FI11
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:11329256, ECO:0000269\|PubMed:2572586, ECO:0000269\|PubMed:7727369, ECO:0000269\|PubMed:8099447, ECO:0007744\|PDB:1F1H, ECO:0007744\|PDB:1F52, ECO:0007744\|PDB:1FPY, ECO:0007744\|PDB:1LGR, ECO:0007744\|PDB:2GLS, ECO:0007744\|PDB:2LGS

Chain	Residue	Details
A	VAL358
J	VAL358
K	VAL358
L	VAL358
B	VAL358
C	VAL358
D	VAL358
E	VAL358
F	VAL358
G	VAL358
H	VAL358
I	VAL358

site_id	SWS_FT_FI12
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:8099447, ECO:0007744\|PDB:2LGS

Chain	Residue	Details
A	PHE360
J	PHE360
K	PHE360
L	PHE360
B	PHE360
C	PHE360
D	PHE360
E	PHE360
F	PHE360
G	PHE360
H	PHE360
I	PHE360

site_id	SWS_FT_FI13
Number of Residues	12
Details	MOD_RES: O-AMP-tyrosine => ECO:0000250\|UniProtKB:P9WN39

Chain	Residue	Details
A	ASP398
J	ASP398
K	ASP398
L	ASP398
B	ASP398
C	ASP398
D	ASP398
E	ASP398
F	ASP398
G	ASP398
H	ASP398
I	ASP398

Catalytic Information from CSA

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

Chain	Residue	Details
A	ARG339
A	ASP50

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1hto

Chain	Residue	Details
J	ARG339
J	ASP50

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1hto

Chain	Residue	Details
K	ARG339
K	ASP50

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1hto

Chain	Residue	Details
L	ARG339
L	ASP50

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

Chain	Residue	Details
B	ARG339
B	ASP50

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

Chain	Residue	Details
C	ARG339
C	ASP50

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

Chain	Residue	Details
D	ARG339
D	ASP50

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

Chain	Residue	Details
E	ARG339
E	ASP50

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

Chain	Residue	Details
F	ARG339
F	ASP50

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

Chain	Residue	Details
G	ARG339
G	ASP50

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

Chain	Residue	Details
H	ARG339
H	ASP50

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1hto

Chain	Residue	Details
I	ARG339
I	ASP50

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