Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1CT9

CRYSTAL STRUCTURE OF ASPARAGINE SYNTHETASE B FROM ESCHERICHIA COLI

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004066	molecular_function	asparagine synthase (glutamine-hydrolyzing) activity
A	0004071	molecular_function	aspartate-ammonia ligase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006541	biological_process	glutamine metabolic process
A	0008652	biological_process	amino acid biosynthetic process
A	0009063	biological_process	amino acid catabolic process
A	0016597	molecular_function	amino acid binding
A	0016874	molecular_function	ligase activity
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0070981	biological_process	L-asparagine biosynthetic process
B	0000166	molecular_function	nucleotide binding
B	0004066	molecular_function	asparagine synthase (glutamine-hydrolyzing) activity
B	0004071	molecular_function	aspartate-ammonia ligase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006541	biological_process	glutamine metabolic process
B	0008652	biological_process	amino acid biosynthetic process
B	0009063	biological_process	amino acid catabolic process
B	0016597	molecular_function	amino acid binding
B	0016874	molecular_function	ligase activity
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0070981	biological_process	L-asparagine biosynthetic process
C	0000166	molecular_function	nucleotide binding
C	0004066	molecular_function	asparagine synthase (glutamine-hydrolyzing) activity
C	0004071	molecular_function	aspartate-ammonia ligase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006541	biological_process	glutamine metabolic process
C	0008652	biological_process	amino acid biosynthetic process
C	0009063	biological_process	amino acid catabolic process
C	0016597	molecular_function	amino acid binding
C	0016874	molecular_function	ligase activity
C	0042802	molecular_function	identical protein binding
C	0042803	molecular_function	protein homodimerization activity
C	0070981	biological_process	L-asparagine biosynthetic process
D	0000166	molecular_function	nucleotide binding
D	0004066	molecular_function	asparagine synthase (glutamine-hydrolyzing) activity
D	0004071	molecular_function	aspartate-ammonia ligase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006541	biological_process	glutamine metabolic process
D	0008652	biological_process	amino acid biosynthetic process
D	0009063	biological_process	amino acid catabolic process
D	0016597	molecular_function	amino acid binding
D	0016874	molecular_function	ligase activity
D	0042802	molecular_function	identical protein binding
D	0042803	molecular_function	protein homodimerization activity
D	0070981	biological_process	L-asparagine biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IUM A 1101

Chain	Residue
A	ASP238
A	ASP351
A	AMP1100
A	IUM1104
A	HOH1312

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE IUM A 1102

Chain	Residue
A	ASP384
A	AMP1100
A	HOH1312
A	GLY349
A	ASP351
A	GLU352
A	TYR357

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IUM A 1103

Chain	Residue
A	GLU352
A	TYR357
A	LYS376
A	ASP384

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IUM A 1104

Chain	Residue
A	SER234
A	ASP238
A	SER239
A	AMP1100
A	IUM1101

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 1105

Chain	Residue
A	TYR149
A	THR170

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IUM B 1108

Chain	Residue
B	ASP238
B	ASP351
B	AMP1107
B	IUM1111

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IUM B 1109

Chain	Residue
B	GLU348
B	GLU352
B	TYR357
B	ASP384
B	AMP1107

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IUM B 1110

Chain	Residue
B	GLU352
B	TYR357
B	LYS376
B	ASP384

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IUM B 1111

Chain	Residue
B	SER234
B	ASP238
B	SER239
B	AMP1107
B	IUM1108

site_id	BC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL B 1112

Chain	Residue
B	THR170

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IUM C 1115

Chain	Residue
C	ASP238
C	ASP351
C	AMP1114
C	IUM1118

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IUM C 1116

Chain	Residue
C	GLU352
C	ASP384
C	AMP1114

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IUM C 1117

Chain	Residue
C	GLU352
C	TYR357
C	LYS376
C	ASP384

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IUM C 1118

Chain	Residue
C	SER234
C	GLY236
C	ASP238
C	AMP1114
C	IUM1115

site_id	BC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL C 1119

Chain	Residue
C	THR170

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE IUM D 1122

Chain	Residue
D	ASP238
D	GLY347
D	ASP351
D	AMP1121
D	IUM1123
D	HOH1278

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IUM D 1123

Chain	Residue
D	GLY349
D	GLU352
D	ASP384
D	IUM1122

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IUM D 1124

Chain	Residue
D	GLU352
D	TYR357
D	ASP384
D	HOH1305

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IUM D 1125

Chain	Residue
D	SER234
D	GLY236
D	SER239
D	AMP1121
D	HOH1278

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL D 1126

Chain	Residue
D	TYR149
D	THR170
D	ILE171
D	LYS172
D	HOH1261

site_id	CC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE AMP A 1100

Chain	Residue
A	IUM1104
A	LEU232
A	LEU233
A	SER234
A	SER239
A	PHE270
A	ALA271
A	VAL272
A	ASP279
A	MET332
A	SER346
A	GLY347
A	GLU348
A	ASP351
A	ASP384
A	IUM1101
A	IUM1102

site_id	CC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GLN A 1106

Chain	Residue
A	ALA1
A	ARG49
A	LEU50
A	ILE52
A	VAL53
A	ASN74
A	GLY75
A	GLU76
A	ASP98
A	HOH1109
A	HOH1133

site_id	CC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE AMP B 1107

Chain	Residue
B	LEU232
B	LEU233
B	SER234
B	ASP238
B	SER239
B	PHE270
B	ALA271
B	VAL272
B	SER346
B	GLY347
B	GLU348
B	ASP351
B	ASP384
B	IUM1108
B	IUM1109
B	IUM1111

site_id	CC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GLN B 1113

Chain	Residue
B	ALA1
B	ARG49
B	LEU50
B	ILE52
B	VAL53
B	ASN74
B	GLY75
B	GLU76
B	ASP98
B	HOH1116
B	HOH1141

site_id	CC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE AMP C 1114

Chain	Residue
C	LEU232
C	LEU233
C	SER234
C	ASP238
C	SER239
C	PHE270
C	ALA271
C	VAL272
C	MET332
C	SER346
C	GLY347
C	GLU348
C	ASP351
C	ASP384
C	ARG387
C	IUM1115
C	IUM1116
C	IUM1118

site_id	CC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GLN C 1120

Chain	Residue
C	ALA1
C	ARG49
C	LEU50
C	ILE52
C	VAL53
C	ASN74
C	GLY75
C	GLU76
C	ASP98
C	CYS99
C	HOH1165

site_id	CC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE AMP D 1121

Chain	Residue
D	LEU232
D	LEU233
D	SER234
D	SER239
D	PHE270
D	ALA271
D	VAL272
D	MET332
D	SER346
D	GLY347
D	GLU348
D	ASP384
D	IUM1122
D	IUM1125

site_id	DC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GLN D 1127

Chain	Residue
D	ALA1
D	ARG49
D	LEU50
D	ILE52
D	VAL53
D	ASN74
D	GLY75
D	GLU76
D	ASP98
D	HOH1155
D	HOH1181

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Site: {"description":"Important for beta-aspartyl-AMP intermediate formation"}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 302

Chain	Residue	Details
A	LEU50	electrostatic stabiliser, hydrogen bond acceptor
A	ASN74	electrostatic stabiliser, hydrogen bond donor
A	GLY75	electrostatic stabiliser, hydrogen bond donor
A	THR321	electrostatic stabiliser, hydrogen bond donor
A	ARG324	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	5
Details	M-CSA 302

Chain	Residue	Details
B	LEU50	electrostatic stabiliser, hydrogen bond acceptor
B	ASN74	electrostatic stabiliser, hydrogen bond donor
B	GLY75	electrostatic stabiliser, hydrogen bond donor
B	THR321	electrostatic stabiliser, hydrogen bond donor
B	ARG324	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA3
Number of Residues	5
Details	M-CSA 302

Chain	Residue	Details
C	LEU50	electrostatic stabiliser, hydrogen bond acceptor
C	ASN74	electrostatic stabiliser, hydrogen bond donor
C	GLY75	electrostatic stabiliser, hydrogen bond donor
C	THR321	electrostatic stabiliser, hydrogen bond donor
C	ARG324	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA4
Number of Residues	5
Details	M-CSA 302

Chain	Residue	Details
D	LEU50	electrostatic stabiliser, hydrogen bond acceptor
D	ASN74	electrostatic stabiliser, hydrogen bond donor
D	GLY75	electrostatic stabiliser, hydrogen bond donor
D	THR321	electrostatic stabiliser, hydrogen bond donor
D	ARG324	electrostatic stabiliser, hydrogen bond donor

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