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4O0G

Crystal structure of the human L-asparaginase protein T219V mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0001917cellular_componentphotoreceptor inner segment
A0003948molecular_functionN4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
A0004067molecular_functionasparaginase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008798molecular_functionbeta-aspartyl-peptidase activity
A0016787molecular_functionhydrolase activity
A0033345biological_processasparagine catabolic process via L-aspartate
B0001917cellular_componentphotoreceptor inner segment
B0003948molecular_functionN4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
B0004067molecular_functionasparaginase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008798molecular_functionbeta-aspartyl-peptidase activity
B0016787molecular_functionhydrolase activity
B0033345biological_processasparagine catabolic process via L-aspartate
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 401
ChainResidue
ALEU55
AGLU56
AASP58
APHE61
AALA63
ACYS65

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 401
ChainResidue
BPHE61
BALA63
BCYS65
BLEU55
BGLU56
BASP58

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:19839645, ECO:0000269|PubMed:22861376
ChainResidueDetails
ATHR168
BTHR168

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AARG196
AVAL219
BARG196
BVAL219

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330
ChainResidueDetails
AMET1
BMET1

223790

PDB entries from 2024-08-14

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