7R57

Escherichia coli type II Asparaginase N24S mutant in its apo form

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

Chain	Residue	Details
A	ILE6-ALA14

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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	ACT_SITE: O-isoaspartyl threonine intermediate => ECO:0000255|PROSITE-ProRule:PRU10099, ECO:0000255|PROSITE-ProRule:PRU10100, ECO:0000269|PubMed:12595697, ECO:0000269|PubMed:1906013, ECO:0000269|PubMed:8434007, ECO:0000269|PubMed:8706862

Chain	Residue	Details
A	THR12
B	THR12
C	THR12
D	THR12

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:12595697, ECO:0000269|PubMed:8434007, ECO:0007744|PDB:1NNS, ECO:0007744|PDB:3ECA

Chain	Residue	Details
A	SER58
A	THR89
B	SER58
B	THR89
C	SER58
C	THR89
D	SER58
D	THR89

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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	THR89	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	LYS162	proton acceptor, proton donor
A	GLU283	electrostatic stabiliser

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site_id	MCSA2
Number of Residues	6
Details	M-CSA 455

Chain	Residue	Details
B	THR12	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
B	TYR25	electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
B	THR89	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	LYS162	proton acceptor, proton donor
B	GLU283	electrostatic stabiliser

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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	THR89	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	LYS162	proton acceptor, proton donor
C	GLU283	electrostatic stabiliser

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site_id	MCSA4
Number of Residues	6
Details	M-CSA 455

Chain	Residue	Details
D	THR12	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
D	TYR25	electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
D	THR89	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	LYS162	proton acceptor, proton donor
D	GLU283	electrostatic stabiliser

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