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6V23

Ligand-free L-aspraginase II from E. coli (EcAII)

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
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
AGLY82-MET92

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
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
ATHR12

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12595697, ECO:0000269|PubMed:8434007, ECO:0007744|PDB:1NNS, ECO:0007744|PDB:3ECA
ChainResidueDetails
ASER58
ATHR89

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 455
ChainResidueDetails
ATHR12covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
ATYR25electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay
ATHR89electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay
AASP90electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor
ALYS162proton acceptor, proton donor
AGLU283electrostatic stabiliser

220113

PDB entries from 2024-05-22

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