Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1BXR

STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE COMPLEXED WITH THE ATP ANALOG AMPPNP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004087	molecular_function	carbamoyl-phosphate synthase (ammonia) activity
A	0004088	molecular_function	carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005951	cellular_component	carbamoyl-phosphate synthase complex
A	0006221	biological_process	pyrimidine nucleotide biosynthetic process
A	0006526	biological_process	L-arginine biosynthetic process
A	0006541	biological_process	glutamine metabolic process
A	0008652	biological_process	amino acid biosynthetic process
A	0016597	molecular_function	amino acid binding
A	0016874	molecular_function	ligase activity
A	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
A	0019856	biological_process	pyrimidine nucleobase biosynthetic process
A	0044205	biological_process	'de novo' UMP biosynthetic process
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0004088	molecular_function	carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
B	0004359	molecular_function	glutaminase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005951	cellular_component	carbamoyl-phosphate synthase complex
B	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
B	0006221	biological_process	pyrimidine nucleotide biosynthetic process
B	0006526	biological_process	L-arginine biosynthetic process
B	0006541	biological_process	glutamine metabolic process
B	0008652	biological_process	amino acid biosynthetic process
B	0016874	molecular_function	ligase activity
B	0019856	biological_process	pyrimidine nucleobase biosynthetic process
B	0044205	biological_process	'de novo' UMP biosynthetic process
B	0046982	molecular_function	protein heterodimerization activity
C	0000166	molecular_function	nucleotide binding
C	0004087	molecular_function	carbamoyl-phosphate synthase (ammonia) activity
C	0004088	molecular_function	carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005951	cellular_component	carbamoyl-phosphate synthase complex
C	0006221	biological_process	pyrimidine nucleotide biosynthetic process
C	0006526	biological_process	L-arginine biosynthetic process
C	0006541	biological_process	glutamine metabolic process
C	0008652	biological_process	amino acid biosynthetic process
C	0016597	molecular_function	amino acid binding
C	0016874	molecular_function	ligase activity
C	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
C	0019856	biological_process	pyrimidine nucleobase biosynthetic process
C	0044205	biological_process	'de novo' UMP biosynthetic process
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0004088	molecular_function	carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
D	0004359	molecular_function	glutaminase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005951	cellular_component	carbamoyl-phosphate synthase complex
D	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
D	0006221	biological_process	pyrimidine nucleotide biosynthetic process
D	0006526	biological_process	L-arginine biosynthetic process
D	0006541	biological_process	glutamine metabolic process
D	0008652	biological_process	amino acid biosynthetic process
D	0016874	molecular_function	ligase activity
D	0019856	biological_process	pyrimidine nucleobase biosynthetic process
D	0044205	biological_process	'de novo' UMP biosynthetic process
D	0046982	molecular_function	protein heterodimerization activity
E	0000166	molecular_function	nucleotide binding
E	0004087	molecular_function	carbamoyl-phosphate synthase (ammonia) activity
E	0004088	molecular_function	carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0005951	cellular_component	carbamoyl-phosphate synthase complex
E	0006221	biological_process	pyrimidine nucleotide biosynthetic process
E	0006526	biological_process	L-arginine biosynthetic process
E	0006541	biological_process	glutamine metabolic process
E	0008652	biological_process	amino acid biosynthetic process
E	0016597	molecular_function	amino acid binding
E	0016874	molecular_function	ligase activity
E	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
E	0019856	biological_process	pyrimidine nucleobase biosynthetic process
E	0044205	biological_process	'de novo' UMP biosynthetic process
E	0046872	molecular_function	metal ion binding
F	0000166	molecular_function	nucleotide binding
F	0004088	molecular_function	carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
F	0004359	molecular_function	glutaminase activity
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0005951	cellular_component	carbamoyl-phosphate synthase complex
F	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
F	0006221	biological_process	pyrimidine nucleotide biosynthetic process
F	0006526	biological_process	L-arginine biosynthetic process
F	0006541	biological_process	glutamine metabolic process
F	0008652	biological_process	amino acid biosynthetic process
F	0016874	molecular_function	ligase activity
F	0019856	biological_process	pyrimidine nucleobase biosynthetic process
F	0044205	biological_process	'de novo' UMP biosynthetic process
F	0046982	molecular_function	protein heterodimerization activity
G	0000166	molecular_function	nucleotide binding
G	0004087	molecular_function	carbamoyl-phosphate synthase (ammonia) activity
G	0004088	molecular_function	carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0005951	cellular_component	carbamoyl-phosphate synthase complex
G	0006221	biological_process	pyrimidine nucleotide biosynthetic process
G	0006526	biological_process	L-arginine biosynthetic process
G	0006541	biological_process	glutamine metabolic process
G	0008652	biological_process	amino acid biosynthetic process
G	0016597	molecular_function	amino acid binding
G	0016874	molecular_function	ligase activity
G	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
G	0019856	biological_process	pyrimidine nucleobase biosynthetic process
G	0044205	biological_process	'de novo' UMP biosynthetic process
G	0046872	molecular_function	metal ion binding
H	0000166	molecular_function	nucleotide binding
H	0004088	molecular_function	carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
H	0004359	molecular_function	glutaminase activity
H	0005515	molecular_function	protein binding
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0005951	cellular_component	carbamoyl-phosphate synthase complex
H	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
H	0006221	biological_process	pyrimidine nucleotide biosynthetic process
H	0006526	biological_process	L-arginine biosynthetic process
H	0006541	biological_process	glutamine metabolic process
H	0008652	biological_process	amino acid biosynthetic process
H	0016874	molecular_function	ligase activity
H	0019856	biological_process	pyrimidine nucleobase biosynthetic process
H	0044205	biological_process	'de novo' UMP biosynthetic process
H	0046982	molecular_function	protein heterodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A 1074

Chain	Residue
A	GLU299
A	ASN301
A	ANP1083
A	HOH1393

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K A 1075

Chain	Residue
A	SER247
A	GLU215
A	ASN236
A	ASP238
A	ALA239
A	ILE242

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K A 1076

Chain	Residue
A	ALA126
A	GLU127
A	GLU299
A	MET300
A	ASN301
A	HOH1199
A	HOH1200

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A 1077

Chain	Residue
A	GLN829
A	GLU841
A	ANP1084
A	HOH1516

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A 1078

Chain	Residue
A	GLU841
A	ASN843
A	ANP1084
A	HOH1308

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K A 1079

Chain	Residue
A	GLU761
A	HIS781
A	GLU783
A	GLN784
A	VAL787
A	SER792

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL A 1080

Chain	Residue
A	ASN371
A	PHE900
A	PRO901
A	GLY902
A	HOH1454

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 1081

Chain	Residue
A	LYS475
A	ASN485
A	HOH1264

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 982

Chain	Residue
A	GLU549
B	ASP114
B	HOH1007

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 1082

Chain	Residue
A	ASN289
A	ASN292
A	ARG294

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K B 984

Chain	Residue
B	HIS16
B	ASP112
B	HOH1009
B	HOH1010
B	HOH1063

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN C 1901

Chain	Residue
C	GLU299
C	ASN301
C	ANP1900
C	HOH4295

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K C 1903

Chain	Residue
C	GLU215
C	ASN236
C	ASP238
C	ALA239
C	ILE242
C	SER247

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K C 1904

Chain	Residue
C	ALA126
C	GLU127
C	GLU299
C	MET300
C	HOH4100
C	HOH4101

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN C 1911

Chain	Residue
C	GLN829
C	GLU841
C	ANP1910
C	HOH4420

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN C 1912

Chain	Residue
C	GLU841
C	ASN843
C	ANP1910
C	HOH4209

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K C 1913

Chain	Residue
C	GLU761
C	HIS781
C	GLU783
C	GLN784
C	VAL787
C	SER792

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL C 1980

Chain	Residue
C	MET174
C	NET1950
C	HOH4293
C	HOH4447
C	HOH4450

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL C 1981

Chain	Residue
C	ALA370
C	ASN371
C	PHE900
C	PRO901
C	GLY902

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL D 1982

Chain	Residue
C	GLU549
C	HOH4183
D	ASP114
D	HOH1217
D	HOH1218

site_id	CC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL C 1983

Chain	Residue
C	ASN289
C	ASN292
C	ARG294

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K D 3984

Chain	Residue
D	HIS16
D	ASP112
D	HOH1529
C	HOH4183

site_id	CC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K C 3985

Chain	Residue
C	THR143
C	ALA144
C	HOH4027

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN C 3986

Chain	Residue
A	HIS680
C	HIS150
C	GLU154
C	HOH4314

site_id	CC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN E 2901

Chain	Residue
E	GLU299
E	ASN301
E	ANP2900
E	HOH3292

site_id	CC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K E 2903

Chain	Residue
E	GLU215
E	ASN236
E	ASP238
E	ALA239
E	ILE242
E	SER247

site_id	CC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE K E 2904

Chain	Residue
E	ALA126
E	GLU127
E	GLU299
E	MET300
E	ASN301
E	HOH3102
E	HOH3103
E	HOH3292

site_id	DC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN E 2911

Chain	Residue
E	GLN829
E	GLU841
E	ANP2910

site_id	DC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN E 2912

Chain	Residue
E	VAL719
E	GLU841
E	ASN843
E	ANP2910
E	HOH3207

site_id	DC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K E 2913

Chain	Residue
E	GLU761
E	HIS781
E	GLU783
E	GLN784
E	VAL787
E	SER792

site_id	DC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL E 2980

Chain	Residue
E	ALA15
E	ILE18
E	ALA23
E	PHE26
E	HOH2992

site_id	DC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL E 2981

Chain	Residue
E	SER854

site_id	DC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K E 2983

Chain	Residue
E	ASP84
E	GLY112
E	THR114
E	HOH3451

site_id	DC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN G 3901

Chain	Residue
G	GLU299
G	ASN301
G	ANP3900
G	HOH4292

site_id	DC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K G 3903

Chain	Residue
G	GLU215
G	ASN236
G	ASP238
G	ALA239
G	ILE242
G	SER247

site_id	DC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K G 3904

Chain	Residue
G	ALA126
G	GLU127
G	GLU299
G	MET300
G	ASN301
G	HOH4105

site_id	EC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN G 3911

Chain	Residue
G	GLN829
G	GLU841
G	ANP3910
G	HOH4408

site_id	EC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN G 3912

Chain	Residue
G	VAL719
G	GLU841
G	ASN843
G	ANP3910
G	HOH4209

site_id	EC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K G 3913

Chain	Residue
G	GLU761
G	HIS781
G	GLU783
G	GLN784
G	VAL787
G	SER792

site_id	EC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL G 3980

Chain	Residue
G	ALA370
G	ASN371
G	PRO901
G	GLY902

site_id	EC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL G 3981

Chain	Residue
G	LYS475

site_id	EC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL G 3982

Chain	Residue
G	LYS941

site_id	EC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL G 3983

Chain	Residue
G	ASN289
G	ASN292

site_id	EC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K H 3987

Chain	Residue
H	HIS16
H	ASP112
H	HOH3529

site_id	EC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K G 3988

Chain	Residue
G	CYS551
G	ASN554
G	HOH4389
G	HOH4390

site_id	FC1
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ANP A 1083

Chain	Residue
A	ARG129
A	ARG169
A	THR173
A	MET174
A	GLY175
A	GLY176
A	ASP207
A	GLU208
A	LEU210
A	ILE211
A	GLU215
A	MET240
A	GLY241
A	ILE242
A	HIS243
A	THR244
A	GLN285
A	GLU299
A	ASN301
A	ARG303
A	ARG306
A	THR376
A	MN1074
A	HOH1132
A	HOH1441
A	HOH1557

site_id	FC2
Number of Residues	28
Details	BINDING SITE FOR RESIDUE ANP A 1084

Chain	Residue
A	ARG675
A	ARG715
A	VAL719
A	LEU720
A	GLY721
A	GLY722
A	MET725
A	ASP753
A	HIS754
A	PHE755
A	LEU756
A	GLU761
A	ALA785
A	GLY786
A	VAL787
A	HIS788
A	SER789
A	GLN829
A	GLU841
A	ASN843
A	ARG845
A	ARG848
A	PRO909
A	MN1077
A	MN1078
A	HOH1308
A	HOH1516
A	HOH1730

site_id	FC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ORN A 1085

Chain	Residue
A	GLU783
A	ASP791
A	ALA793
A	GLU892
A	LEU907
A	TYR1040
A	ASP1041
A	THR1042
A	HOH1345
A	HOH1362

site_id	FC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NET A 1086

Chain	Residue
A	GLN22
A	GLN93
A	THR94
A	ASN936

site_id	FC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ANP C 1900

Chain	Residue
C	ARG129
C	ILE167
C	ARG169
C	MET174
C	GLY175
C	GLY176
C	GLU208
C	SER209
C	LEU210
C	ILE211
C	GLU215
C	MET240
C	GLY241
C	ILE242
C	HIS243
C	THR244
C	GLN285
C	GLU299
C	ASN301
C	ARG303
C	ARG306
C	THR376
C	MN1901
C	HOH4031
C	HOH4295

site_id	FC6
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ANP C 1910

Chain	Residue
C	ARG675
C	ARG715
C	VAL719
C	LEU720
C	GLY721
C	GLY722
C	MET725
C	ASP753
C	HIS754
C	PHE755
C	LEU756
C	GLU761
C	GLY786
C	VAL787
C	HIS788
C	SER789
C	GLN829
C	GLU841
C	ASN843
C	ARG845
C	ARG848
C	PRO909
C	MN1911
C	MN1912
C	HOH4420

site_id	FC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ORN C 1920

Chain	Residue
C	GLU783
C	ASP791
C	GLU892
C	VAL893
C	LEU907
C	TYR1040
C	ASP1041
C	THR1042
C	HOH4246
C	HOH4263

site_id	FC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NET C 1950

Chain	Residue
C	GLN22
C	THR94
C	ASN936
C	CL1980
C	HOH4000

site_id	FC9
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ANP E 2900

Chain	Residue
E	ARG129
E	ARG169
E	THR173
E	MET174
E	GLY175
E	GLY176
E	GLU208
E	LEU210
E	ILE211
E	GLU215
E	MET240
E	GLY241
E	ILE242
E	HIS243
E	THR244
E	GLN285
E	GLU299
E	ASN301
E	ARG303
E	ARG306
E	THR376
E	MN2901
E	HOH3033
E	HOH3341

site_id	GC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ANP E 2910

Chain	Residue
E	ARG675
E	ARG715
E	VAL719
E	LEU720
E	GLY721
E	GLY722
E	MET725
E	ASP753
E	HIS754
E	PHE755
E	LEU756
E	GLU761
E	ALA785
E	GLY786
E	VAL787
E	HIS788
E	SER789
E	GLN829
E	GLU841
E	ASN843
E	ARG845
E	ARG848
E	MN2911
E	MN2912
E	HOH3414

site_id	GC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ORN E 2920

Chain	Residue
E	GLU783
E	ASP791
E	GLU892
E	LEU907
E	TYR1040
E	ASP1041
E	THR1042
E	HOH3244
E	HOH3261

site_id	GC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NET E 2950

Chain	Residue
E	GLN22
E	THR94
E	ASN936

site_id	GC4
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ANP G 3900

Chain	Residue
G	ARG129
G	ILE167
G	ARG169
G	THR173
G	MET174
G	GLY175
G	GLY176
G	GLU208
G	LEU210
G	ILE211
G	GLU215
G	MET240
G	GLY241
G	ILE242
G	HIS243
G	THR244
G	GLN285
G	GLU299
G	ASN301
G	ARG303
G	ARG306
G	THR376
G	MN3901
G	HOH4037
G	HOH4292
G	HOH4338

site_id	GC5
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ANP G 3910

Chain	Residue
G	ARG675
G	ARG715
G	VAL719
G	LEU720
G	GLY721
G	GLY722
G	MET725
G	ASP753
G	HIS754
G	PHE755
G	LEU756
G	GLU761
G	ALA785
G	GLY786
G	VAL787
G	HIS788
G	SER789
G	GLN829
G	ILE840
G	GLU841
G	ASN843
G	ARG845
G	ARG848
G	MN3911
G	MN3912
G	HOH4408

site_id	GC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ORN G 3920

Chain	Residue
G	GLU783
G	ASP791
G	GLU892
G	LEU907
G	TYR1040
G	ASP1041
G	THR1042
G	HOH4245

site_id	GC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NET G 3950

Chain	Residue
G	GLN22
G	THR94
G	ASN97
G	ASN936
G	HOH4005
G	HOH4270

Functional Information from PROSITE/UniProt

site_id	PS00866
Number of Residues	15
Details	CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. FPCIIRPSftmGGsG

Chain	Residue	Details
A	PHE164-GLY178
A	TYR710-ALA724

site_id	PS00867
Number of Residues	8
Details	CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. VIEMNPRV

Chain	Residue	Details
A	VAL297-VAL304
A	LEU839-ALA846

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	780
Details	Domain: {"description":"ATP-grasp 1","evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	764
Details	Domain: {"description":"ATP-grasp 2","evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	544
Details	Domain: {"description":"MGS-like","evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1604
Details	Region: {"description":"Carboxyphosphate synthetic domain","evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	596
Details	Region: {"description":"Oligomerization domain","evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1528
Details	Region: {"description":"Carbamoyl phosphate synthetic domain","evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	544
Details	Region: {"description":"Allosteric domain","evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	72
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10029528","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A9X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1C30","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1C3O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1CE8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1CS0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JDB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KEE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M6V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T36","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10428826","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CE8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10029528","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10089390","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10428826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10587438","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9636022","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CE8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10428826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9636022","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CE8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10029528","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10089390","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10428826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9636022","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CE8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10029528","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10089390","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	748
Details	Domain: {"description":"Glutamine amidotransferase type-1","evidences":[{"source":"HAMAP-Rule","id":"MF_01209","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01209","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	8
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01209","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01209","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10587438","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1C3O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 10029528

Chain	Residue	Details
B	HIS353
B	CYS269

site_id	CSA2
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 10029528

Chain	Residue	Details
D	HIS353
D	CYS269

site_id	CSA3
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 10029528

Chain	Residue	Details
F	HIS353
F	CYS269

site_id	CSA4
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 10029528

Chain	Residue	Details
H	HIS353
H	CYS269

site_id	MCSA1
Number of Residues	3
Details	M-CSA 435

Chain	Residue	Details
B	CYS269	covalent catalysis, proton shuttle (general acid/base)
A	ARG303	electrostatic stabiliser
A	ARG715	electrostatic stabiliser
A	GLY721	electrostatic stabiliser
A	GLY722	electrostatic stabiliser
A	GLU761	steric role
A	GLN829	metal ligand
A	GLU841	metal ligand
A	ASN843	metal ligand
A	ARG848	electrostatic stabiliser
B	HIS353	proton shuttle (general acid/base)
B	GLU355	steric role
A	GLU215	steric role
A	HIS243	proton shuttle (general acid/base)
A	ASN283	electrostatic stabiliser
A	GLN285	metal ligand
A	GLU299	metal ligand
A	ASN301	metal ligand

site_id	MCSA2
Number of Residues	3
Details	M-CSA 435

Chain	Residue	Details
D	CYS269	covalent catalysis, proton shuttle (general acid/base)
C	ARG303	electrostatic stabiliser
C	ARG715	electrostatic stabiliser
C	GLY721	electrostatic stabiliser
C	GLY722	electrostatic stabiliser
C	GLU761	steric role
C	GLN829	metal ligand
C	GLU841	metal ligand
C	ASN843	metal ligand
C	ARG848	electrostatic stabiliser
D	HIS353	proton shuttle (general acid/base)
D	GLU355	steric role
C	GLU215	steric role
C	HIS243	proton shuttle (general acid/base)
C	ASN283	electrostatic stabiliser
C	GLN285	metal ligand
C	GLU299	metal ligand
C	ASN301	metal ligand

site_id	MCSA3
Number of Residues	3
Details	M-CSA 435

Chain	Residue	Details
F	CYS269	covalent catalysis, proton shuttle (general acid/base)
E	ARG303	electrostatic stabiliser
E	ARG715	electrostatic stabiliser
E	GLY721	electrostatic stabiliser
E	GLY722	electrostatic stabiliser
E	GLU761	steric role
E	GLN829	metal ligand
E	GLU841	metal ligand
E	ASN843	metal ligand
E	ARG848	electrostatic stabiliser
F	HIS353	proton shuttle (general acid/base)
F	GLU355	steric role
E	GLU215	steric role
E	HIS243	proton shuttle (general acid/base)
E	ASN283	electrostatic stabiliser
E	GLN285	metal ligand
E	GLU299	metal ligand
E	ASN301	metal ligand

site_id	MCSA4
Number of Residues	3
Details	M-CSA 435

Chain	Residue	Details
H	CYS269	covalent catalysis, proton shuttle (general acid/base)
G	ARG303	electrostatic stabiliser
G	ARG715	electrostatic stabiliser
G	GLY721	electrostatic stabiliser
G	GLY722	electrostatic stabiliser
G	GLU761	steric role
G	GLN829	metal ligand
G	GLU841	metal ligand
G	ASN843	metal ligand
G	ARG848	electrostatic stabiliser
H	HIS353	proton shuttle (general acid/base)
H	GLU355	steric role
G	GLU215	steric role
G	HIS243	proton shuttle (general acid/base)
G	ASN283	electrostatic stabiliser
G	GLN285	metal ligand
G	GLU299	metal ligand
G	ASN301	metal ligand

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