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3LJQ

Crystal Structure of the Glycosylasparaginase T152C apo-precursor

Functional Information from GO Data
ChainGOidnamespacecontents
A0003948molecular_functionN4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A0042597cellular_componentperiplasmic space
C0003948molecular_functionN4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
C0005737cellular_componentcytoplasm
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0016787molecular_functionhydrolase activity
C0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
C0042597cellular_componentperiplasmic space
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GLY C 596
ChainResidue
CASP451
CHOH654
CGLY472
CMET473
CARG480
CASP483
CSER484
CGLY504
CGLY506
CHOH625

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 597
ChainResidue
AVAL42
AGLU43
AASP45
AGLU48
AVAL51
ATYR53

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA C 597
ChainResidue
CVAL342
CASP345
CGLU348
CVAL351
CTYR353

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10490104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17157318","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20800597","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9685368","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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