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6V2G

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004067molecular_functionasparaginase activity
A0006528biological_processasparagine metabolic process
A0006530biological_processL-asparagine 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_processL-asparagine 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_processL-asparagine 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
D0006528biological_processasparagine metabolic process
D0006530biological_processL-asparagine 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 PROSITE/UniProt
site_idPS00917
Number of Residues11
DetailsASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GfVitHGTDTM
ChainResidueDetails
AGLY82-MET92

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
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
AAEI12
BAEI12
CAEI12
DAEI12

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:12595697, ECO:0000269|PubMed:8434007, ECO:0007744|PDB:1NNS, ECO:0007744|PDB:3ECA
ChainResidueDetails
ASER58
ATHR89
BSER58
BTHR89
CSER58
CTHR89
DSER58
DTHR89

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 455
ChainResidueDetails
AAEI12covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
ALYS29electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
AGLU93electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
AGLU94electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
ATHR166proton acceptor, proton donor
AALA287electrostatic stabiliser

site_idMCSA2
Number of Residues6
DetailsM-CSA 455
ChainResidueDetails
BAEI12covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
BLYS29electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
BGLU93electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
BGLU94electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
BTHR166proton acceptor, proton donor
BALA287electrostatic stabiliser

site_idMCSA3
Number of Residues6
DetailsM-CSA 455
ChainResidueDetails
CAEI12covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
CLYS29electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
CGLU93electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
CGLU94electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
CTHR166proton acceptor, proton donor
CALA287electrostatic stabiliser

site_idMCSA4
Number of Residues6
DetailsM-CSA 455
ChainResidueDetails
DAEI12covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
DLYS29electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
DGLU93electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
DGLU94electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
DTHR166proton acceptor, proton donor
DALA287electrostatic stabiliser

237992

PDB entries from 2025-06-25

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