Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6PA6

ECAII(T89V,K162T) MUTANT IN COMPLEX WITH L-ASN AT PH 8.3 in space group C2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004067	molecular_function	asparaginase activity
A	0006520	biological_process	amino acid metabolic process
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	0006520	biological_process	amino acid metabolic process
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	0006520	biological_process	amino acid metabolic process
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	0006520	biological_process	amino acid metabolic process
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	12
Details	binding site for residue ASN A 401

Chain	Residue
A	GLY11
A	HOH620
B	ASN248
B	GLU283
A	THR12
A	GLY57
A	SER58
A	GLN59
A	GLY88
A	VAL89
A	ASP90
A	ALA114

site_id	AC2
Number of Residues	13
Details	binding site for residue ASN B 401

Chain	Residue
A	ASN248
A	GLU283
B	GLY11
B	THR12
B	GLY57
B	SER58
B	GLN59
B	GLY88
B	VAL89
B	ASP90
B	ALA114
B	HOH581
B	HOH613

site_id	AC3
Number of Residues	4
Details	binding site for residue IMD B 402

Chain	Residue
B	ILE4
B	THR5
B	ASN47
B	LYS49

site_id	AC4
Number of Residues	12
Details	binding site for residue ASN C 401

Chain	Residue
C	GLY11
C	THR12
C	GLY57
C	SER58
C	GLN59
C	GLY88
C	VAL89
C	ASP90
C	ALA114
C	HOH647
D	ASN248
D	GLU283

site_id	AC5
Number of Residues	6
Details	binding site for residue IMD C 402

Chain	Residue
C	ASN3
C	ILE4
C	THR5
C	ASN47
C	LYS49
C	THR80

site_id	AC6
Number of Residues	13
Details	binding site for residue ASN D 401

Chain	Residue
C	ASN248
C	GLU283
D	GLY11
D	THR12
D	GLY57
D	SER58
D	GLN59
D	GLY88
D	VAL89
D	ASP90
D	ALA114
D	HOH535
D	HOH640

site_id	AC7
Number of Residues	6
Details	binding site for residue IMD D 402

Chain	Residue
D	ASN3
D	ILE4
D	THR5
D	ASN47
D	LYS49
D	THR80

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE6-ALA14

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	648
Details	Domain: {"description":"Asparaginase/glutaminase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01068","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
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_FI3
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	THR12	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
A	TYR25	electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
A	VAL89	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
A	ASP90	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
A	THR162	proton acceptor, proton donor
A	GLU283	electrostatic stabiliser

site_id	MCSA2
Number of Residues	5
Details	M-CSA 455

Chain	Residue	Details
B	THR12	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
B	VAL89	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
B	ASP90	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
B	THR162	proton acceptor, proton donor
B	GLU283	electrostatic stabiliser

site_id	MCSA3
Number of Residues	6
Details	M-CSA 455

Chain	Residue	Details
C	THR12	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
C	TYR25	electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
C	VAL89	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
C	ASP90	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
C	THR162	proton acceptor, proton donor
C	GLU283	electrostatic stabiliser

site_id	MCSA4
Number of Residues	5
Details	M-CSA 455

Chain	Residue	Details
D	THR12	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
D	VAL89	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
D	ASP90	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
D	THR162	proton acceptor, proton donor
D	GLU283	electrostatic stabiliser

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