1IHD

Crystal Structure of Trigonal Form of D90E Mutant of Escherichia coli Asparaginase II

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
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

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	2
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	4
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	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 3eca

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 3eca

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 3eca

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 3eca

Chain	Residue	Details
A	THR12	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
A	THR89	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
A	GLU90	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
A	LYS162	proton acceptor, proton donor
A	GLU283	electrostatic stabiliser

Chain

Residue

Details