Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6V24

Complex of mutant (K162M) of E. coli L-asparaginase II with L-Asp. Covalent acyl-enzyme intermediate.

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
B	0004067	molecular_function	asparaginase activity
B	0006528	biological_process	asparagine metabolic process
B	0006530	biological_process	L-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	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
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	L-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	14
Details	binding site for residue ASP A 401

Chain	Residue
A	GLY11
A	ASP90
A	ALA114
A	HOH658
C	ASN248
C	GLU283
A	THR12
A	TYR25
A	VAL27
A	GLY57
A	SER58
A	GLN59
A	GLY88
A	THR89

site_id	AC2
Number of Residues	20
Details	binding site for Di-peptide GLY C 11 and AEI C 12

Chain	Residue
A	ASN248
A	GLU283
C	GLY10
C	ILE13
C	ALA14
C	GLY15
C	TYR25
C	VAL27
C	GLY28
C	ILE56
C	GLY57
C	SER58
C	GLN59
C	GLY88
C	THR89
C	ASP90
C	ALA114
C	PRO117
C	HOH444
C	HOH540

site_id	AC3
Number of Residues	19
Details	binding site for Di-peptide AEI C 12 and ILE C 13

Chain	Residue
A	ASN248
A	GLU283
C	GLY10
C	GLY11
C	ALA14
C	GLY15
C	TYR25
C	VAL27
C	GLY57
C	SER58
C	GLN59
C	GLY88
C	THR89
C	ASP90
C	ALA114
C	PRO117
C	HOH444
C	HOH489
C	HOH540

site_id	AC4
Number of Residues	22
Details	binding site for Di-peptide GLY D 11 and AEI D 12

Chain	Residue
B	ASN248
B	GLU283
D	GLY10
D	ILE13
D	ALA14
D	GLY15
D	TYR25
D	VAL27
D	GLY28
D	ILE56
D	GLY57
D	SER58
D	GLN59
D	GLY88
D	THR89
D	ASP90
D	ALA114
D	ARG116
D	PRO117
D	SER118
D	ASP401
D	HOH606

site_id	AC5
Number of Residues	20
Details	binding site for Di-peptide AEI D 12 and ILE D 13

Chain	Residue
B	ASN248
B	GLU283
D	GLY10
D	GLY11
D	ALA14
D	GLY15
D	TYR25
D	GLY57
D	SER58
D	GLN59
D	GLY88
D	THR89
D	ASP90
D	ALA114
D	ARG116
D	PRO117
D	SER118
D	ASP401
D	HOH606
D	HOH648

site_id	AC6
Number of Residues	19
Details	binding site for Di-peptide ASP D 401 and AEI D 12

Chain	Residue
D	ALA14
D	GLY15
D	TYR25
D	VAL27
D	GLY57
D	SER58
D	GLN59
D	GLY88
D	THR89
D	ASP90
D	ALA114
D	ARG116
D	PRO117
D	SER118
D	HOH606
B	ASN248
B	GLU283
D	GLY11
D	ILE13

site_id	AC7
Number of Residues	19
Details	binding site for Di-peptide ASP D 401 and AEI D 12

Chain	Residue
B	ASN248
B	GLU283
D	GLY11
D	ILE13
D	ALA14
D	GLY15
D	TYR25
D	VAL27
D	GLY57
D	SER58
D	GLN59
D	GLY88
D	THR89
D	ASP90
D	ALA114
D	ARG116
D	PRO117
D	SER118
D	HOH606

site_id	AC8
Number of Residues	19
Details	binding site for Di-peptide ASP D 401 and AEI D 12

Chain	Residue
B	ASN248
B	GLU283
D	GLY11
D	ILE13
D	ALA14
D	GLY15
D	TYR25
D	VAL27
D	GLY57
D	SER58
D	GLN59
D	GLY88
D	THR89
D	ASP90
D	ALA114
D	ARG116
D	PRO117
D	SER118
D	HOH606

site_id	AC9
Number of Residues	19
Details	binding site for Di-peptide ASP D 401 and AEI D 12

Chain	Residue
B	ASN248
B	GLU283
D	GLY11
D	ILE13
D	ALA14
D	GLY15
D	TYR25
D	VAL27
D	GLY57
D	SER58
D	GLN59
D	GLY88
D	THR89
D	ASP90
D	ALA114
D	ARG116
D	PRO117
D	SER118
D	HOH606

site_id	AD1
Number of Residues	19
Details	binding site for Di-peptide ASP D 401 and AEI D 12

Chain	Residue
B	ASN248
B	GLU283
D	GLY11
D	ILE13
D	ALA14
D	GLY15
D	TYR25
D	VAL27
D	GLY57
D	SER58
D	GLN59
D	GLY88
D	THR89
D	ASP90
D	ALA114
D	ARG116
D	PRO117
D	SER118
D	HOH606

site_id	AD2
Number of Residues	19
Details	binding site for Di-peptide ASP D 401 and AEI D 12

Chain	Residue
B	ASN248
B	GLU283
D	GLY11
D	ILE13
D	ALA14
D	GLY15
D	TYR25
D	VAL27
D	GLY57
D	SER58
D	GLN59
D	GLY88
D	THR89
D	ASP90
D	ALA114
D	ARG116
D	PRO117
D	SER118
D	HOH606

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
B	GLY82-MET92
A	GLY82-MET92

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	648
Details	Domain: {"description":"Asparaginase/glutaminase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01068","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
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_FI3
Number of Residues	8
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	MCSA1
Number of Residues	6
Details	M-CSA 455

Chain	Residue	Details
B	AEI12	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
B	LYS29	electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
B	GLU93	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
B	GLU94	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
B	THR166	proton acceptor, proton donor
B	ALA287	electrostatic stabiliser

site_id	MCSA2
Number of Residues	6
Details	M-CSA 455

Chain	Residue	Details
C	AEI12	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
C	LYS29	electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
C	GLU93	electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
C	GLU94	electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
C	THR166	proton acceptor, proton donor
C	ALA287	electrostatic stabiliser

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