Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2P2D

Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia coli L-Asparaginase I

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	0008152	biological_process	metabolic process
A	0016787	molecular_function	hydrolase activity
A	0033345	biological_process	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	0008152	biological_process	metabolic process
B	0016787	molecular_function	hydrolase activity
B	0033345	biological_process	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	0008152	biological_process	metabolic process
C	0016787	molecular_function	hydrolase activity
C	0033345	biological_process	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	0008152	biological_process	metabolic process
D	0016787	molecular_function	hydrolase activity
D	0033345	biological_process	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	9
Details	BINDING SITE FOR RESIDUE GOL A 7001

Chain	Residue
A	SER102
A	LEU105
A	ASN107
A	LEU108
A	PRO196
A	ARG331
A	HOH9027
A	HOH9030
A	HOH9098

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 7002

Chain	Residue
C	ASN176
C	THR271
C	MET274
C	SER275
C	GLY276
C	MET300
C	HOH9014
C	HOH9121

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 7003

Chain	Residue
C	SER102
C	LEU105
C	LEU108
C	PRO196
C	ARG331
C	HOH9038
C	HOH9052
C	HOH9089

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 7004

Chain	Residue
A	ARG240
A	THR271
A	CYS273
A	MET300
A	VAL302
A	HOH9017
A	HOH9059

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL D 7005

Chain	Residue
D	SER102
D	LEU105
D	ASN107
D	LEU108
D	PRO196
D	ARG331
D	HOH9031
D	HOH9038
D	HOH9044

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 7006

Chain	Residue
D	ASN176
D	MET274
D	SER275
D	GLY276
D	MET300
D	HOH9025
D	HOH9116

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 7007

Chain	Residue
B	SER102
B	LEU105
B	LEU108
B	PRO196
B	ARG331
B	HOH9048
B	HOH9052
B	HOH9068

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 7008

Chain	Residue
B	ASN176
B	THR271
B	MET274
B	SER275
B	GLY276
B	MET300
B	HOH9029
B	HOH9033

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 9001

Chain	Residue
A	GLY13
A	MET58
A	SER60
A	GLY90
A	THR91
A	ASP92
A	HOH9083
A	HOH9166

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 9002

Chain	Residue
B	GLY13
B	THR14
B	ASP59
B	SER60
B	GLY90
B	THR91
B	ASP92
B	HOH9138

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL C 9003

Chain	Residue
C	GLY13
C	THR14
C	MET58
C	ASP59
C	SER60
C	GLY90
C	THR91
C	ASP92
C	HOH9132

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL D 9004

Chain	Residue
D	GLY13
D	MET58
D	ASP59
D	SER60
D	GLY90
D	THR91
D	ASP92
D	HOH9062
D	HOH9134

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	ACT_SITE: O-isoaspartyl threonine intermediate => ECO:0000255\|PROSITE-ProRule:PRU10099, ECO:0000255\|PROSITE-ProRule:PRU10100, ECO:0000269\|PubMed:17451745

Chain	Residue	Details
A	THR14
B	THR14
C	THR14
D	THR14

site_id	SWS_FT_FI2
Number of Residues	20
Details	BINDING: BINDING => ECO:0007744\|PDB:2P2N

Chain	Residue	Details
A	ASP59
B	THR271
C	ASP59
C	THR91
C	THR162
C	ARG240
C	THR271
D	ASP59
D	THR91
D	THR162
D	ARG240
A	THR91
D	THR271
A	THR162
A	ARG240
A	THR271
B	ASP59
B	THR91
B	THR162
B	ARG240

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