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6V24

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004067molecular_functionasparaginase activity
A0006520biological_processamino acid metabolic process
A0006528biological_processasparagine metabolic process
A0006530biological_processasparagine catabolic process
A0016787molecular_functionhydrolase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0032991cellular_componentprotein-containing complex
A0042597cellular_componentperiplasmic space
A0042802molecular_functionidentical protein binding
A0051289biological_processprotein homotetramerization
B0004067molecular_functionasparaginase activity
B0006528biological_processasparagine metabolic process
B0006530biological_processasparagine catabolic process
B0016787molecular_functionhydrolase activity
B0030288cellular_componentouter membrane-bounded periplasmic space
B0032991cellular_componentprotein-containing complex
B0042597cellular_componentperiplasmic space
B0042802molecular_functionidentical protein binding
B0051289biological_processprotein homotetramerization
C0004067molecular_functionasparaginase activity
C0006528biological_processasparagine metabolic process
C0006530biological_processasparagine catabolic process
C0016787molecular_functionhydrolase activity
C0030288cellular_componentouter membrane-bounded periplasmic space
C0032991cellular_componentprotein-containing complex
C0042597cellular_componentperiplasmic space
C0042802molecular_functionidentical protein binding
C0051289biological_processprotein homotetramerization
D0004067molecular_functionasparaginase activity
D0006520biological_processamino acid metabolic process
D0006528biological_processasparagine metabolic process
D0006530biological_processasparagine catabolic process
D0016787molecular_functionhydrolase activity
D0030288cellular_componentouter membrane-bounded periplasmic space
D0032991cellular_componentprotein-containing complex
D0042597cellular_componentperiplasmic space
D0042802molecular_functionidentical protein binding
D0051289biological_processprotein homotetramerization
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue ASP A 401
ChainResidue
AGLY11
AASP90
AALA114
AHOH658
CASN248
CGLU283
ATHR12
ATYR25
AVAL27
AGLY57
ASER58
AGLN59
AGLY88
ATHR89

site_idAC2
Number of Residues20
Detailsbinding site for Di-peptide GLY C 11 and AEI C 12
ChainResidue
AASN248
AGLU283
CGLY10
CILE13
CALA14
CGLY15
CTYR25
CVAL27
CGLY28
CILE56
CGLY57
CSER58
CGLN59
CGLY88
CTHR89
CASP90
CALA114
CPRO117
CHOH444
CHOH540

site_idAC3
Number of Residues19
Detailsbinding site for Di-peptide AEI C 12 and ILE C 13
ChainResidue
AASN248
AGLU283
CGLY10
CGLY11
CALA14
CGLY15
CTYR25
CVAL27
CGLY57
CSER58
CGLN59
CGLY88
CTHR89
CASP90
CALA114
CPRO117
CHOH444
CHOH489
CHOH540

site_idAC4
Number of Residues22
Detailsbinding site for Di-peptide GLY D 11 and AEI D 12
ChainResidue
BASN248
BGLU283
DGLY10
DILE13
DALA14
DGLY15
DTYR25
DVAL27
DGLY28
DILE56
DGLY57
DSER58
DGLN59
DGLY88
DTHR89
DASP90
DALA114
DARG116
DPRO117
DSER118
DASP401
DHOH606

site_idAC5
Number of Residues20
Detailsbinding site for Di-peptide AEI D 12 and ILE D 13
ChainResidue
BASN248
BGLU283
DGLY10
DGLY11
DALA14
DGLY15
DTYR25
DGLY57
DSER58
DGLN59
DGLY88
DTHR89
DASP90
DALA114
DARG116
DPRO117
DSER118
DASP401
DHOH606
DHOH648

site_idAC6
Number of Residues19
Detailsbinding site for Di-peptide ASP D 401 and AEI D 12
ChainResidue
DALA14
DGLY15
DTYR25
DVAL27
DGLY57
DSER58
DGLN59
DGLY88
DTHR89
DASP90
DALA114
DARG116
DPRO117
DSER118
DHOH606
BASN248
BGLU283
DGLY11
DILE13

site_idAC7
Number of Residues19
Detailsbinding site for Di-peptide ASP D 401 and AEI D 12
ChainResidue
BASN248
BGLU283
DGLY11
DILE13
DALA14
DGLY15
DTYR25
DVAL27
DGLY57
DSER58
DGLN59
DGLY88
DTHR89
DASP90
DALA114
DARG116
DPRO117
DSER118
DHOH606

site_idAC8
Number of Residues19
Detailsbinding site for Di-peptide ASP D 401 and AEI D 12
ChainResidue
BASN248
BGLU283
DGLY11
DILE13
DALA14
DGLY15
DTYR25
DVAL27
DGLY57
DSER58
DGLN59
DGLY88
DTHR89
DASP90
DALA114
DARG116
DPRO117
DSER118
DHOH606

site_idAC9
Number of Residues19
Detailsbinding site for Di-peptide ASP D 401 and AEI D 12
ChainResidue
BASN248
BGLU283
DGLY11
DILE13
DALA14
DGLY15
DTYR25
DVAL27
DGLY57
DSER58
DGLN59
DGLY88
DTHR89
DASP90
DALA114
DARG116
DPRO117
DSER118
DHOH606

site_idAD1
Number of Residues19
Detailsbinding site for Di-peptide ASP D 401 and AEI D 12
ChainResidue
BASN248
BGLU283
DGLY11
DILE13
DALA14
DGLY15
DTYR25
DVAL27
DGLY57
DSER58
DGLN59
DGLY88
DTHR89
DASP90
DALA114
DARG116
DPRO117
DSER118
DHOH606

site_idAD2
Number of Residues19
Detailsbinding site for Di-peptide ASP D 401 and AEI D 12
ChainResidue
BASN248
BGLU283
DGLY11
DILE13
DALA14
DGLY15
DTYR25
DVAL27
DGLY57
DSER58
DGLN59
DGLY88
DTHR89
DASP90
DALA114
DARG116
DPRO117
DSER118
DHOH606

Functional Information from PROSITE/UniProt
site_idPS00144
Number of Residues9
DetailsASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. IlATGGTIA
ChainResidueDetails
AILE6-ALA14

site_idPS00917
Number of Residues11
DetailsASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GfVitHGTDTM
ChainResidueDetails
BGLY82-MET92
AGLY82-MET92

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_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
ChainResidueDetails
BAEI12
CAEI12

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12595697, ECO:0000269|PubMed:8434007, ECO:0007744|PDB:1NNS, ECO:0007744|PDB:3ECA
ChainResidueDetails
BSER58
BTHR89
CSER58
CTHR89

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 455
ChainResidueDetails
BAEI12covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
BTYR25electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
BTHR89electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
BASP90electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
BMET162proton acceptor, proton donor
BGLU283electrostatic stabiliser

site_idMCSA2
Number of Residues6
DetailsM-CSA 455
ChainResidueDetails
CAEI12covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
CTYR25electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
CTHR89electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
CASP90electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
CMET162proton acceptor, proton donor
CGLU283electrostatic stabiliser

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PDB entries from 2024-10-30

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