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1AGX

REFINED CRYSTAL STRUCTURE OF ACINETOBACTER GLUTAMINASIFICANS GLUTAMINASE-ASPARAGINASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004067molecular_functionasparaginase activity
A0004359molecular_functionglutaminase activity
A0006520biological_processamino acid metabolic process
A0006528biological_processasparagine metabolic process
A0016787molecular_functionhydrolase activity
A0042597cellular_componentperiplasmic space
A0050417molecular_functionglutamin-(asparagin-)ase activity
Functional Information from PROSITE/UniProt
site_idPS00144
Number of Residues9
DetailsASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. IvATGGTIA
ChainResidueDetails
AILE6-ALA14

site_idPS00917
Number of Residues11
DetailsASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GvVitHGTDTM
ChainResidueDetails
AGLY85-MET95

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10099, ECO:0000255|PROSITE-ProRule:PRU10100
ChainResidueDetails
ATHR12

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER59
ATHR92

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
ATHR92
ATHR12
ATYR26

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
AGLU288

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
ATHR92
AASP93
ALYS165
ATHR12
ATYR26

224004

PDB entries from 2024-08-21

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