6NX6

ECAII(D90T,K162T) MUTANT IN COMPLEX WITH CITRATE AT PH 5

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue ACY A 401

Chain	Residue
A	GLY57
A	SER58
A	HOH590

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site_id	AC2
Number of Residues	9
Details	binding site for residue CIT B 401

Chain	Residue
B	HOH558
B	HOH588
B	HOH599
A	HIS-1
A	HIS0
B	GLY11
B	GLY57
B	SER58
B	GLY88

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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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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
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

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site_id	SWS_FT_FI2
Number of Residues	4
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

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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	THR90	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
A	THR162	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	THR90	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
B	THR162	proton acceptor, proton donor
B	GLU283	electrostatic stabiliser

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