Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2HIM

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	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	8
Details	BINDING SITE FOR RESIDUE ASP A 7001

Chain	Residue
A	GLY13
A	THR14
A	ASP59
A	SER60
A	GLY90
A	THR91
A	ASP92
A	SER117

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ASP B 7002

Chain	Residue
B	THR14
B	ASP59
B	SER60
B	GLY90
B	THR91
B	ASP92
B	SER117
B	GLY13

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ASP C 7003

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

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ASP D 7004

Chain	Residue
D	GLY13
D	THR14
D	ASP59
D	SER60
D	GLY90
D	THR91
D	ASP92
D	SER117
D	HOH5032

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ASN A 8001

Chain	Residue
A	ALA162
A	ARG240
A	THR271
A	GLN272
A	CYS273
A	THR301
A	VAL302
A	GLU303
A	HOH5249
A	EDO9002
C	ARG240

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ASN B 8002

Chain	Residue
B	ALA162
B	ARG240
B	THR271
B	GLN272
B	CYS273
B	THR301
B	VAL302
B	GLU303
B	HOH5398
B	EDO9004
D	ARG240
D	HOH5101

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ASN C 8003

Chain	Residue
A	ARG240
C	ALA162
C	ARG240
C	THR271
C	GLN272
C	CYS273
C	MET274
C	THR301
C	VAL302
C	GLU303
C	HOH5220
C	EDO9001

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ASN D 8004

Chain	Residue
B	ARG240
D	ALA162
D	ARG240
D	THR271
D	GLN272
D	CYS273
D	THR301
D	VAL302
D	GLU303
D	HOH5151
D	HOH5389
D	EDO9003

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ASN A 6001

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

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ASN B 6002

Chain	Residue
D	ASN246
B	GLY13
B	THR14
B	MET17
B	ASP59
B	SER60
B	SER61
B	GLY90
B	THR91
B	ASP92

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ASN C 6003

Chain	Residue
A	ASN246
C	GLY13
C	THR14
C	MET17
C	ASP59
C	SER60
C	SER61
C	GLY90
C	THR91
C	ASP92

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ASN D 6004

Chain	Residue
B	ASN246
D	GLY13
D	THR14
D	ASP59
D	SER60
D	SER61
D	GLY90
D	THR91
D	ASP92

site_id	BC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EDO C 9001

Chain	Residue
C	ASN176
C	THR271
C	CYS273
C	MET274
C	SER275
C	GLY276
C	ASP299
C	MET300
C	THR301
C	ASN8003

site_id	BC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EDO A 9002

Chain	Residue
A	ASN176
A	THR271
A	CYS273
A	MET274
A	SER275
A	GLY276
A	ASP299
A	MET300
A	THR301
A	ASN8001

site_id	BC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO D 9003

Chain	Residue
D	ASN176
D	THR271
D	CYS273
D	MET274
D	SER275
D	GLY276
D	ASP299
D	MET300
D	ASN8004

site_id	BC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EDO B 9004

Chain	Residue
B	ASN176
B	THR271
B	CYS273
B	MET274
B	SER275
B	GLY276
B	ASP299
B	MET300
B	THR301
B	ASN8002

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 9005

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

site_id	BC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO B 9006

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

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 9007

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

site_id	CC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO D 9008

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

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 3eca

Chain	Residue	Details
A	ASP92
A	THR14
A	THR91
A	LYS163

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 3eca

Chain	Residue	Details
B	ASP92
B	THR14
B	THR91
B	LYS163

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 3eca

Chain	Residue	Details
C	ASP92
C	THR14
C	THR91
C	LYS163

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 3eca

Chain	Residue	Details
D	ASP92
D	THR14
D	THR91
D	LYS163

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 3eca

Chain	Residue	Details
A	LEU289
C	THR14
C	THR91

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 3eca

Chain	Residue	Details
D	THR14
D	THR91
B	LEU289

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 3eca

Chain	Residue	Details
A	THR14
A	THR91
C	LEU289

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 3eca

Chain	Residue	Details
D	LEU289
B	THR14
B	THR91

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