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1P4V

CRYSTAL STRUCTURE OF THE GLYCOSYLASPARAGINASE PRECURSOR D151N MUTANT WITH GLYCINE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003948molecular_functionN4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
A0004067molecular_functionasparaginase activity
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008798molecular_functionbeta-aspartyl-peptidase activity
A0016787molecular_functionhydrolase activity
A0042597cellular_componentperiplasmic space
C0003948molecular_functionN4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
C0004067molecular_functionasparaginase activity
C0005737cellular_componentcytoplasm
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0008798molecular_functionbeta-aspartyl-peptidase activity
C0016787molecular_functionhydrolase activity
C0042597cellular_componentperiplasmic space
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GLY A 296
ChainResidue
ATHR152
AGLY172
AMET173
AARG180
AASP183
ASER184
AGLY204
AGLY206
AHOH301

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GLY C 596
ChainResidue
CHOH7
CHOH10
CTHR452
CGLY472
CMET473
CARG480
CASP483
CSER484
CGLY504
CGLY506

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:10490104, ECO:0000269|PubMed:17157318, ECO:0000269|PubMed:20800597, ECO:0000269|PubMed:9685368
ChainResidueDetails
ATHR152
CTHR452

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AARG180
ATHR203
CARG480
CTHR503

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1apy
ChainResidueDetails
AGLY204
ATHR152
ATHR170
ASER50
ATHR203

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1apy
ChainResidueDetails
CSER350
CTHR452
CGLY504
CTHR503
CTHR470

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PDB entries from 2024-07-17

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