Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6NXC

ECAI(T162A) MUTANT 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	11
Details	binding site for residue CIT A 9101

Chain	Residue
A	GLY13
A	HOH9248
C	ASN246
A	THR14
A	ASP59
A	SER60
A	SER61
A	GLY90
A	THR91
A	ASP92
A	SER117

site_id	AC2
Number of Residues	3
Details	binding site for residue EDO A 9102

Chain	Residue
A	HIS52
A	ASP74
A	HIS78

site_id	AC3
Number of Residues	10
Details	binding site for residue EDO A 9103

Chain	Residue
A	ASN176
A	THR271
A	CYS273
A	MET274
A	SER275
A	GLY276
A	ASP299
A	MET300
A	THR301
A	ASN9109

site_id	AC4
Number of Residues	4
Details	binding site for residue CL A 9104

Chain	Residue
A	HIS165
A	ALA166
A	ASP167
C	SER275

site_id	AC5
Number of Residues	9
Details	binding site for residue GOL A 9105

Chain	Residue
A	ASP92
A	GLN118
A	LYS163
A	ALA166
A	HOH9201
B	ILE185
C	GLY243
C	VAL244
C	ASN246

site_id	AC6
Number of Residues	2
Details	binding site for residue CL A 9106

Chain	Residue
A	ASN107
A	GLY198

site_id	AC7
Number of Residues	6
Details	binding site for residue EDO A 9107

Chain	Residue
A	ARG240
A	GLN272
C	TYR96
C	ARG240
C	VAL302
C	ASN402

site_id	AC8
Number of Residues	5
Details	binding site for residue CL A 9108

Chain	Residue
A	SER275
A	GLY276
C	HIS165
C	ALA166
C	ASP167

site_id	AC9
Number of Residues	12
Details	binding site for residue ASN A 9109

Chain	Residue
A	ALA162
A	ARG240
A	THR271
A	GLN272
A	CYS273
A	THR301
A	VAL302
A	GLU303
A	EDO9103
A	HOH9252
C	ARG240
C	EDO401

site_id	AD1
Number of Residues	12
Details	binding site for residue ASN B 9102

Chain	Residue
B	ALA162
B	ARG240
B	THR271
B	GLN272
B	CYS273
B	THR301
B	VAL302
B	GLU303
B	EDO9104
B	HOH9216
B	HOH9233
D	ARG240

site_id	AD2
Number of Residues	7
Details	binding site for residue EDO B 9103

Chain	Residue
B	HIS0
B	GLN2
B	LYS3
B	PRO44
B	GLU45
B	MET46
B	CL9106

site_id	AD3
Number of Residues	10
Details	binding site for residue EDO B 9104

Chain	Residue
B	ASN176
B	THR271
B	CYS273
B	MET274
B	SER275
B	GLY276
B	ASP299
B	MET300
B	THR301
B	ASN9102

site_id	AD4
Number of Residues	8
Details	binding site for residue EDO B 9105

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

site_id	AD5
Number of Residues	4
Details	binding site for residue CL B 9106

Chain	Residue
B	LYS4
B	PRO47
B	EDO9103
B	HOH9250

site_id	AD6
Number of Residues	4
Details	binding site for residue CL B 9107

Chain	Residue
B	ALA166
B	ASP167
D	SER275
D	HOH654

site_id	AD7
Number of Residues	4
Details	binding site for residue CL B 9108

Chain	Residue
B	SER275
D	HIS165
D	ALA166
D	ASP167

site_id	AD8
Number of Residues	7
Details	binding site for residue EDO C 401

Chain	Residue
A	TYR96
A	ARG240
A	VAL302
A	ASN9109
C	THR216
C	ARG240
C	GLN272

site_id	AD9
Number of Residues	11
Details	binding site for residue ASN C 402

Chain	Residue
A	ARG240
A	EDO9107
C	ALA162
C	ARG240
C	THR271
C	CYS273
C	THR301
C	VAL302
C	GLU303
C	EDO404
C	HOH524

site_id	AE1
Number of Residues	9
Details	binding site for residue EDO C 404

Chain	Residue
C	ASN176
C	THR271
C	MET274
C	SER275
C	GLY276
C	ASP299
C	MET300
C	THR301
C	ASN402

site_id	AE2
Number of Residues	7
Details	binding site for residue EDO C 405

Chain	Residue
A	GLY243
A	VAL244
A	ASN246
C	ASP92
C	GLN118
C	LYS163
C	ALA166

site_id	AE3
Number of Residues	3
Details	binding site for residue CL C 406

Chain	Residue
C	GLN69
C	HIS70
C	GLU73

site_id	AE4
Number of Residues	1
Details	binding site for residue CL D 401

Chain	Residue
D	ARG33

site_id	AE5
Number of Residues	12
Details	binding site for residue ASN D 402

Chain	Residue
B	ARG240
D	ALA162
D	ARG240
D	THR271
D	GLN272
D	CYS273
D	THR301
D	VAL302
D	GLU303
D	EDO406
D	HOH542
D	HOH554

site_id	AE6
Number of Residues	3
Details	binding site for residue CL D 404

Chain	Residue
D	LYS4
D	PRO47
D	HOH544

site_id	AE7
Number of Residues	1
Details	binding site for residue CL D 405

Chain	Residue
D	GLU201

site_id	AE8
Number of Residues	9
Details	binding site for residue EDO D 406

Chain	Residue
D	ASN176
D	THR271
D	CYS273
D	MET274
D	SER275
D	GLY276
D	ASP299
D	MET300
D	ASN402

site_id	AE9
Number of Residues	8
Details	binding site for residue EDO D 407

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

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)