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5V2I

Crystal structure of a mutant glycosylasparaginase (G172D) that causes the genetic disease Aspartylglucosaminuria

Functional Information from GO Data
ChainGOidnamespacecontents
A0003948molecular_functionN4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
A0004067molecular_functionasparaginase activity
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0006517biological_processprotein deglycosylation
A0008233molecular_functionpeptidase activity
A0008798molecular_functionbeta-aspartyl-peptidase activity
A0016787molecular_functionhydrolase activity
A0042597cellular_componentperiplasmic space
B0003948molecular_functionN4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
B0004067molecular_functionasparaginase activity
B0005737cellular_componentcytoplasm
B0006508biological_processproteolysis
B0006517biological_processprotein deglycosylation
B0008233molecular_functionpeptidase activity
B0008798molecular_functionbeta-aspartyl-peptidase activity
B0016787molecular_functionhydrolase activity
B0042597cellular_componentperiplasmic space
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
BTHR152

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AARG180
ATHR203
BARG180
BTHR203

224201

PDB entries from 2024-08-28

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