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4OSY

STRUCTURE of FULLY-CLEAVED GLYCINE-BOUND HUMAN L-ASPARAGINASE PROTEIN

Replaces:  4HLP
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
Details
ChainResidue
ALEU55
AGLU56
AASP58
APHE61
AALA63
ACYS65

site_idAC2
Number of Residues11
Details
ChainResidue
AARG196
AASP199
ASER200
AGLY220
AGLY222
AHOH517
AHOH551
AHOH573
ATHR168
ATHR186
AGLY188

site_idAC3
Number of Residues7
Details
ChainResidue
ASER88
AALA89
AVAL108
AMET109
ATHR112
AHIS114
BLYS227

site_idAC4
Number of Residues6
Details
ChainResidue
BLEU55
BGLU56
BASP58
BPHE61
BALA63
BCYS65

site_idAC5
Number of Residues9
Details
ChainResidue
ALYS227
BSER88
BALA89
BVAL108
BMET109
BTHR112
BPRO113
BHIS114
BCYS115

site_idAC6
Number of Residues8
Details
ChainResidue
BTHR168
BILE189
BARG196
BGLY198
BASP199
BSER200
BGLY220
BGLY222

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
ATHR219
BARG196
BTHR219

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

220113

PDB entries from 2024-05-22

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