Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6V28

Complex of double mutant (T89V,K162T) of E. coli L-asparaginase II with L-Asp

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004067	molecular_function	asparaginase activity
A	0006528	biological_process	asparagine metabolic process
A	0006530	biological_process	L-asparagine catabolic process
A	0016787	molecular_function	hydrolase activity
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0032991	cellular_component	protein-containing complex
A	0042597	cellular_component	periplasmic space
A	0042802	molecular_function	identical protein binding
A	0051289	biological_process	protein homotetramerization
B	0004067	molecular_function	asparaginase activity
B	0006528	biological_process	asparagine metabolic process
B	0006530	biological_process	L-asparagine catabolic process
B	0016787	molecular_function	hydrolase activity
B	0030288	cellular_component	outer membrane-bounded periplasmic space
B	0032991	cellular_component	protein-containing complex
B	0042597	cellular_component	periplasmic space
B	0042802	molecular_function	identical protein binding
B	0051289	biological_process	protein homotetramerization
C	0004067	molecular_function	asparaginase activity
C	0006528	biological_process	asparagine metabolic process
C	0006530	biological_process	L-asparagine catabolic process
C	0016787	molecular_function	hydrolase activity
C	0030288	cellular_component	outer membrane-bounded periplasmic space
C	0032991	cellular_component	protein-containing complex
C	0042597	cellular_component	periplasmic space
C	0042802	molecular_function	identical protein binding
C	0051289	biological_process	protein homotetramerization
D	0004067	molecular_function	asparaginase activity
D	0006528	biological_process	asparagine metabolic process
D	0006530	biological_process	L-asparagine catabolic process
D	0016787	molecular_function	hydrolase activity
D	0030288	cellular_component	outer membrane-bounded periplasmic space
D	0032991	cellular_component	protein-containing complex
D	0042597	cellular_component	periplasmic space
D	0042802	molecular_function	identical protein binding
D	0051289	biological_process	protein homotetramerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue IMD A 401

Chain	Residue
A	ASN3
A	ILE4
A	THR5
A	ASN47
A	LYS49
A	LYS79
A	THR80

site_id	AC2
Number of Residues	12
Details	binding site for residue GOL B 901

Chain	Residue
B	GLY10
B	GLY11
B	ALA14
B	GLY28
B	VAL30
B	GLY31
B	VAL32
B	GLN52
B	ASN55
B	HOH1042
B	ALA8
B	THR9

site_id	AC3
Number of Residues	9
Details	binding site for residue GOL C 901

Chain	Residue
C	ASP286
C	ALA287
C	GLY290
C	PHE291
C	PRO316
C	GLN317
C	GLN320
C	HOH1012
C	HOH1081

site_id	AC4
Number of Residues	11
Details	binding site for residue GOL C 902

Chain	Residue
C	ASN209
C	ASN209
C	HOH1250
C	HOH1250
D	PHE254
D	PHE254
D	ASP255
D	ASP255
D	TYR289
D	TYR289
D	HOH670

site_id	AC5
Number of Residues	3
Details	binding site for residue GOL D 401

Chain	Residue
C	SER224
C	LEU226
D	TYR236

site_id	AC6
Number of Residues	4
Details	binding site for residue GOL D 402

Chain	Residue
D	SER173
D	GLY177
D	TYR181
D	HOH706

site_id	AC7
Number of Residues	11
Details	binding site for residue GOL D 403

Chain	Residue
D	ALA8
D	THR9
D	GLY10
D	GLY11
D	ALA14
D	VAL30
D	GLY31
D	VAL32
D	GLN52
D	ASN55
D	HOH524

site_id	AC8
Number of Residues	6
Details	binding site for residue GOL D 404

Chain	Residue
D	PHE291
D	GLN317
D	GLN320
D	HOH513
D	HOH661
D	HOH749

site_id	AC9
Number of Residues	6
Details	binding site for residue IMD D 405

Chain	Residue
D	ASN3
D	ILE4
D	THR5
D	ASN47
D	LYS79
D	THR80

site_id	AD1
Number of Residues	19
Details	binding site for Di-peptide GLY B 11 and AEI B 12

Chain	Residue
A	ASN248
A	GLU283
B	GLY10
B	ILE13
B	ALA14
B	GLY15
B	TYR25
B	VAL27
B	ILE56
B	GLY57
B	SER58
B	GLN59
B	GLY88
B	VAL89
B	ASP90
B	ALA114
B	ARG116
B	GOL901
B	HOH1109

site_id	AD2
Number of Residues	19
Details	binding site for Di-peptide AEI B 12 and ILE B 13

Chain	Residue
B	GLY88
B	VAL89
B	ASP90
B	ALA114
B	ARG116
B	SER118
B	HOH1004
B	HOH1109
A	ASN248
A	GLU283
B	GLY10
B	GLY11
B	ALA14
B	GLY15
B	TYR25
B	LEU35
B	GLY57
B	SER58
B	GLN59

site_id	AD3
Number of Residues	18
Details	binding site for Di-peptide GLY C 11 and AEI C 12

Chain	Residue
C	GLY10
C	ILE13
C	ALA14
C	GLY15
C	TYR25
C	ILE56
C	GLY57
C	SER58
C	GLN59
C	GLY88
C	VAL89
C	ASP90
C	ALA114
C	ARG116
C	PRO117
C	HOH1170
D	ASN248
D	GLU283

site_id	AD4
Number of Residues	19
Details	binding site for Di-peptide AEI C 12 and ILE C 13

Chain	Residue
C	GLY10
C	GLY11
C	ALA14
C	GLY15
C	TYR25
C	LEU35
C	GLY57
C	SER58
C	GLN59
C	GLY88
C	VAL89
C	ASP90
C	ALA114
C	ARG116
C	PRO117
C	HOH1163
C	HOH1170
D	ASN248
D	GLU283

site_id	AD5
Number of Residues	18
Details	binding site for Di-peptide GLY D 11 and AEI D 12

Chain	Residue
C	ASN248
C	GLU283
D	GLY10
D	ILE13
D	ALA14
D	GLY15
D	TYR25
D	VAL27
D	ILE56
D	GLY57
D	SER58
D	GLN59
D	GLY88
D	VAL89
D	ASP90
D	ALA114
D	GOL403
D	HOH674

site_id	AD6
Number of Residues	18
Details	binding site for Di-peptide AEI D 12 and ILE D 13

Chain	Residue
C	ASN248
C	GLU283
D	GLY10
D	GLY11
D	ALA14
D	GLY15
D	TYR25
D	VAL27
D	LEU35
D	GLY57
D	SER58
D	GLN59
D	GLY88
D	VAL89
D	ASP90
D	ALA114
D	HOH596
D	HOH674

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":"12595697","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1906013","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8434007","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8706862","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12595697","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8434007","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NNS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ECA","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 455

Chain	Residue	Details
A	AEI12	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
A	LYS29	electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
A	GLU93	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
A	GLU94	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
A	THR166	proton acceptor, proton donor
A	ALA287	electrostatic stabiliser

site_id	MCSA2
Number of Residues	6
Details	M-CSA 455

Chain	Residue	Details
B	AEI12	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
B	LYS29	electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
B	GLU93	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
B	GLU94	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
B	THR166	proton acceptor, proton donor
B	ALA287	electrostatic stabiliser

site_id	MCSA3
Number of Residues	6
Details	M-CSA 455

Chain	Residue	Details
C	AEI12	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
C	LYS29	electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
C	GLU93	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
C	GLU94	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
C	THR166	proton acceptor, proton donor
C	ALA287	electrostatic stabiliser

site_id	MCSA4
Number of Residues	6
Details	M-CSA 455

Chain	Residue	Details
D	AEI12	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
D	LYS29	electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
D	GLU93	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
D	GLU94	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
D	THR166	proton acceptor, proton donor
D	ALA287	electrostatic stabiliser

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