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2ZAL

Crystal structure of E. coli isoaspartyl aminopeptidase/L-asparaginase in complex with L-aspartate

Replaces:  1SEO
Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
B0016787molecular_functionhydrolase activity
C0016787molecular_functionhydrolase activity
D0016787molecular_functionhydrolase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"18323626","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15946951","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZAL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1apy
ChainResidueDetails
AASN67

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1apy
ChainResidueDetails
CASN67

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1apy
ChainResidueDetails
AGLY69
BTHR179
BGLY231
BTHR197
BTHR230

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1apy
ChainResidueDetails
CGLY69
DTHR179
DGLY231
DTHR197
DTHR230

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PDB entries from 2025-12-17

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