Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6UOG

Asparaginase II from Escherichia coli

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
E	0004067	molecular_function	asparaginase activity
E	0006520	biological_process	amino acid metabolic process
E	0006528	biological_process	asparagine metabolic process
E	0006530	biological_process	asparagine catabolic process
E	0016787	molecular_function	hydrolase activity
E	0030288	cellular_component	outer membrane-bounded periplasmic space
E	0032991	cellular_component	protein-containing complex
E	0042597	cellular_component	periplasmic space
E	0042802	molecular_function	identical protein binding
E	0051289	biological_process	protein homotetramerization
F	0004067	molecular_function	asparaginase activity
F	0006520	biological_process	amino acid metabolic process
F	0006528	biological_process	asparagine metabolic process
F	0006530	biological_process	asparagine catabolic process
F	0016787	molecular_function	hydrolase activity
F	0030288	cellular_component	outer membrane-bounded periplasmic space
F	0032991	cellular_component	protein-containing complex
F	0042597	cellular_component	periplasmic space
F	0042802	molecular_function	identical protein binding
F	0051289	biological_process	protein homotetramerization
G	0004067	molecular_function	asparaginase activity
G	0006520	biological_process	amino acid metabolic process
G	0006528	biological_process	asparagine metabolic process
G	0006530	biological_process	asparagine catabolic process
G	0016787	molecular_function	hydrolase activity
G	0030288	cellular_component	outer membrane-bounded periplasmic space
G	0032991	cellular_component	protein-containing complex
G	0042597	cellular_component	periplasmic space
G	0042802	molecular_function	identical protein binding
G	0051289	biological_process	protein homotetramerization
H	0004067	molecular_function	asparaginase activity
H	0006520	biological_process	amino acid metabolic process
H	0006528	biological_process	asparagine metabolic process
H	0006530	biological_process	asparagine catabolic process
H	0016787	molecular_function	hydrolase activity
H	0030288	cellular_component	outer membrane-bounded periplasmic space
H	0032991	cellular_component	protein-containing complex
H	0042597	cellular_component	periplasmic space
H	0042802	molecular_function	identical protein binding
H	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

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

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
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
E	THR12
F	THR12
G	THR12
H	THR12

site_id	SWS_FT_FI2
Number of Residues	16
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
E	SER58
E	THR89
F	SER58
F	THR89
G	SER58
G	THR89
H	SER58
H	THR89

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	LYS162	proton acceptor, proton donor
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	GLU283	electrostatic stabiliser

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	LYS162	proton acceptor, proton donor
B	THR89	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
B	TYR25	electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
B	ASP90	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, 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	THR89	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
C	TYR25	electrostatic stabiliser, increase nucleophilicity, 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

site_id	MCSA4
Number of Residues	6
Details	M-CSA 455

Chain	Residue	Details
D	THR89	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
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	ASP90	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
D	LYS162	proton acceptor, proton donor
D	GLU283	electrostatic stabiliser

site_id	MCSA5
Number of Residues	6
Details	M-CSA 455

Chain	Residue	Details
E	THR89	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
E	THR12	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
E	TYR25	electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
E	ASP90	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
E	LYS162	proton acceptor, proton donor
E	GLU283	electrostatic stabiliser

site_id	MCSA6
Number of Residues	6
Details	M-CSA 455

Chain	Residue	Details
F	THR89	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
F	THR12	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
F	TYR25	electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
F	ASP90	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
F	LYS162	proton acceptor, proton donor
F	GLU283	electrostatic stabiliser

site_id	MCSA7
Number of Residues	6
Details	M-CSA 455

Chain	Residue	Details
G	THR89	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
G	THR12	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
G	TYR25	electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
G	ASP90	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
G	LYS162	proton acceptor, proton donor
G	GLU283	electrostatic stabiliser

site_id	MCSA8
Number of Residues	6
Details	M-CSA 455

Chain	Residue	Details
H	THR89	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
H	THR12	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
H	TYR25	electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
H	ASP90	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
H	LYS162	proton acceptor, proton donor
H	GLU283	electrostatic stabiliser

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