6V2C

Complex of mutant (K162M) of E. coli L-asparaginase II with L-Asp. Covalent acyl-enzyme intermediate and tetrahedral intermediate

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 PROSITE/UniProt

site_id	PS00917
Number of Residues	11
Details	ASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GfVitHGTDTM

Chain	Residue	Details
A	GLY82-MET92

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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

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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

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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

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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

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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

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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

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