Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6NXD

TYPE I L-ASPARAGINASE FROM ESCHERICHIA COLI IN COMPLEX WITH CITRATE AT PH 4

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004067	molecular_function	asparaginase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006520	biological_process	amino acid metabolic process
A	0016787	molecular_function	hydrolase activity
A	0033345	biological_process	L-asparagine catabolic process via L-aspartate
A	0042802	molecular_function	identical protein binding
A	0051289	biological_process	protein homotetramerization
B	0003824	molecular_function	catalytic activity
B	0004067	molecular_function	asparaginase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006520	biological_process	amino acid metabolic process
B	0016787	molecular_function	hydrolase activity
B	0033345	biological_process	L-asparagine catabolic process via L-aspartate
B	0042802	molecular_function	identical protein binding
B	0051289	biological_process	protein homotetramerization
C	0003824	molecular_function	catalytic activity
C	0004067	molecular_function	asparaginase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006520	biological_process	amino acid metabolic process
C	0016787	molecular_function	hydrolase activity
C	0033345	biological_process	L-asparagine catabolic process via L-aspartate
C	0042802	molecular_function	identical protein binding
C	0051289	biological_process	protein homotetramerization
D	0003824	molecular_function	catalytic activity
D	0004067	molecular_function	asparaginase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006520	biological_process	amino acid metabolic process
D	0016787	molecular_function	hydrolase activity
D	0033345	biological_process	L-asparagine catabolic process via L-aspartate
D	0042802	molecular_function	identical protein binding
D	0051289	biological_process	protein homotetramerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue CL A 1001

Chain	Residue
A	SER275
C	ASP167
C	GLY168

site_id	AC2
Number of Residues	3
Details	binding site for residue CL A 1002

Chain	Residue
A	ASP167
A	GLY168
C	SER275

site_id	AC3
Number of Residues	3
Details	binding site for residue CL A 1003

Chain	Residue
A	ASN107
A	GLY198
A	EDO1007

site_id	AC4
Number of Residues	3
Details	binding site for residue CL A 1004

Chain	Residue
A	GLN69
A	HIS70
A	GLU73

site_id	AC5
Number of Residues	11
Details	binding site for residue CIT A 1005

Chain	Residue
A	GLY13
A	THR14
A	ASP59
A	SER60
A	SER61
A	GLY90
A	THR91
A	ASP92
A	SER117
A	HOH1144
C	ASN246

site_id	AC6
Number of Residues	13
Details	binding site for residue ASN A 1006

Chain	Residue
A	THR162
A	ARG240
A	THR271
A	GLN272
A	CYS273
A	THR301
A	VAL302
A	GLU303
A	EDO1008
A	HOH1151
A	HOH1186
C	ARG240
C	EDO1005

site_id	AC7
Number of Residues	5
Details	binding site for residue EDO A 1007

Chain	Residue
A	ASN145
A	PRO196
A	HIS197
A	CL1003
A	HOH1160

site_id	AC8
Number of Residues	10
Details	binding site for residue EDO A 1008

Chain	Residue
A	ASN176
A	THR271
A	CYS273
A	MET274
A	SER275
A	GLY276
A	ASP299
A	MET300
A	THR301
A	ASN1006

site_id	AC9
Number of Residues	6
Details	binding site for residue EDO A 1009

Chain	Residue
A	ARG240
A	GLN272
C	ARG240
C	VAL302
C	ASN1003
C	HOH1144

site_id	AD1
Number of Residues	7
Details	binding site for residue CL B 1001

Chain	Residue
B	SER275
B	GLY276
B	HOH1241
D	HIS165
D	ALA166
D	ASP167
D	GLY168

site_id	AD2
Number of Residues	5
Details	binding site for residue CL B 1002

Chain	Residue
B	HIS165
B	ALA166
B	ASP167
B	GLY168
D	SER275

site_id	AD3
Number of Residues	3
Details	binding site for residue CL B 1003

Chain	Residue
B	LYS4
B	PRO47
B	EDO1008

site_id	AD4
Number of Residues	2
Details	binding site for residue CL B 1004

Chain	Residue
B	GLY200
B	GLU201

site_id	AD5
Number of Residues	13
Details	binding site for residue ASN B 1006

Chain	Residue
B	THR162
B	ARG240
B	THR271
B	GLN272
B	CYS273
B	THR301
B	VAL302
B	GLU303
B	EDO1007
B	HOH1155
D	ARG240
D	EDO1008
D	HOH1161

site_id	AD6
Number of Residues	7
Details	binding site for residue EDO B 1007

Chain	Residue
B	ASN176
B	THR271
B	CYS273
B	MET274
B	SER275
B	GLY276
B	ASN1006

site_id	AD7
Number of Residues	6
Details	binding site for residue EDO B 1008

Chain	Residue
B	CL1003
B	HIS0
B	GLN2
B	LYS3
B	PRO44
B	GLU45

site_id	AD8
Number of Residues	6
Details	binding site for residue EDO B 1009

Chain	Residue
B	ARG240
B	GLN272
D	TYR96
D	ARG240
D	ASN1003
D	HOH1140

site_id	AD9
Number of Residues	3
Details	binding site for residue CL C 1001

Chain	Residue
C	ASN107
C	GLY198
C	HOH1211

site_id	AE1
Number of Residues	12
Details	binding site for residue ASN C 1003

Chain	Residue
A	ARG240
A	EDO1009
C	THR162
C	ARG240
C	THR271
C	GLN272
C	CYS273
C	THR301
C	VAL302
C	GLU303
C	EDO1004
C	HOH1128

site_id	AE2
Number of Residues	10
Details	binding site for residue EDO C 1004

Chain	Residue
C	ASN176
C	THR271
C	CYS273
C	MET274
C	SER275
C	GLY276
C	ASP299
C	MET300
C	THR301
C	ASN1003

site_id	AE3
Number of Residues	7
Details	binding site for residue EDO C 1005

Chain	Residue
A	TYR96
A	ARG240
A	VAL302
A	ASN1006
A	HOH1128
C	ARG240
C	GLN272

site_id	AE4
Number of Residues	4
Details	binding site for residue CL D 1001

Chain	Residue
D	LYS4
D	PRO47
D	EDO1007
D	HOH1130

site_id	AE5
Number of Residues	12
Details	binding site for residue ASN D 1003

Chain	Residue
B	ARG240
B	EDO1009
D	THR162
D	ARG240
D	THR271
D	GLN272
D	CYS273
D	THR301
D	VAL302
D	GLU303
D	EDO1004
D	HOH1158

site_id	AE6
Number of Residues	8
Details	binding site for residue EDO D 1004

Chain	Residue
D	ASN176
D	THR271
D	CYS273
D	MET274
D	SER275
D	GLY276
D	MET300
D	ASN1003

site_id	AE7
Number of Residues	8
Details	binding site for residue EDO D 1005

Chain	Residue
B	GLY243
B	VAL244
B	ASN246
C	ILE185
D	ASP92
D	GLN118
D	LYS163
D	ALA166

site_id	AE8
Number of Residues	4
Details	binding site for residue EDO D 1006

Chain	Residue
D	PRO-4
D	ASN145
D	HIS197
D	HOH1169

site_id	AE9
Number of Residues	4
Details	binding site for residue EDO D 1007

Chain	Residue
D	HIS0
D	LYS3
D	PRO44
D	CL1001

site_id	AF1
Number of Residues	7
Details	binding site for residue EDO D 1008

Chain	Residue
B	TYR96
B	ARG240
B	ASN1006
D	ARG240
D	GLN272
D	HOH1133
D	HOH1161

Functional Information from PROSITE/UniProt

site_id	PS00144
Number of Residues	9
Details	ASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. VaYTGGTIG

Chain	Residue	Details
A	VAL8-GLY16

site_id	PS00917
Number of Residues	11
Details	ASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GfVilHGTDTM

Chain	Residue	Details
A	GLY84-MET94

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"O-isoaspartyl threonine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10099","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10100","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17451745","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PDB","id":"2P2N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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