6PA2

E. coli L-asparaginase II mutant (K162M) in complex with L-Asp at pH 5.6

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 PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue ASP A 401

Chain	Residue
A	GLY11
A	HOH647
C	GLU283
A	THR12
A	GLY57
A	SER58
A	GLN59
A	GLY88
A	THR89
A	ASP90
A	ALA114

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site_id	AC2
Number of Residues	12
Details	binding site for residue ASP C 401

Chain	Residue
A	GLU283
C	GLY11
C	THR12
C	GLY57
C	SER58
C	GLN59
C	GLY88
C	THR89
C	ASP90
C	ALA114
C	HOH643
C	HOH659

---

site_id	AC3
Number of Residues	15
Details	binding site for residue ASP B 401

Chain	Residue
B	GLY11
B	THR12
B	TYR25
B	VAL27
B	GLY57
B	SER58
B	GLN59
B	GLY88
B	THR89
B	ASP90
B	ALA114
B	HOH682
B	HOH690
D	ASN248
D	GLU283

---

site_id	AC4
Number of Residues	10
Details	binding site for residue GOL B 402

Chain	Residue
B	ASP106
B	LYS107
B	PRO108
B	SER141
B	ALA142
B	ASN143
B	HOH503
B	HOH523
B	HOH632
B	HOH670

---

site_id	AC5
Number of Residues	12
Details	binding site for residue ASP D 401

Chain	Residue
B	ASN248
B	GLU283
D	GLY11
D	THR12
D	GLY57
D	SER58
D	GLN59
D	GLY88
D	THR89
D	ASP90
D	ALA114
D	HOH663

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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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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
C	THR12
B	THR12
D	THR12

---

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
C	SER58
C	THR89
B	SER58
B	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	THR89	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
A	TYR25	electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
A	ASP90	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
A	MET162	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
C	ASP90	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
C	MET162	proton acceptor, proton donor
C	THR89	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
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	GLU283	electrostatic stabiliser

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site_id	MCSA3
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	MET162	proton acceptor, proton donor
B	ASP90	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
B	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	THR89	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
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	MET162	proton acceptor, proton donor
D	GLU283	electrostatic stabiliser

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