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3TKJ

Crystal Structure of Human Asparaginase-like Protein 1 Thr168Ala

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 Residues7
DetailsBINDING SITE FOR RESIDUE TAM A 402
ChainResidue
AARG39
AHOH607
BASP57
BASN100
AGLY1
AASN2
APRO3

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
ATHR186
AGLY188
AARG196
AGLY198
AASP199
ASER200
AGLY222
AHOH604

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 401
ChainResidue
BLEU55
BGLU56
BASP58
BPHE61
BALA63
BCYS65

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE TAM B 402
ChainResidue
BASN2
BPRO3
BTYR35
BARG39
BLYS289
BASP290

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 403
ChainResidue
BTHR186
BGLY188
BARG196
BGLY198
BASP199
BSER200
BGLY222
BHOH595
BHOH596

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:19839645, ECO:0000269|PubMed:22861376
ChainResidueDetails
AALA168
BALA168

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AARG196
ATHR219
BARG196
BTHR219

218853

PDB entries from 2024-04-24

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