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PDBsum entry 4pvs
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PDB id:
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Hydrolase
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Title:
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Crystal structure of fully-cleaved human l-asparaginase protein in complex with l-aspartate
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Structure:
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Isoaspartyl peptidase/l-asparaginase. Chain: a, b. Synonym: asparaginase-like protein 1, beta-aspartyl-peptidase, isoaspartyl dipeptidase, l-asparagine amidohydrolase, isoaspartyl peptidase/l-asparaginase alpha chain, isoaspartyl peptidase/l- asparaginase beta chain. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: alp, asrgl1, crash. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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1.84Å
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R-factor:
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0.171
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R-free:
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0.216
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Authors:
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J.Nomme,A.Lavie
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Key ref:
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J.Nomme
et al.
(2012).
Structures of apo and product-bound human L-asparaginase: insights into the mechanism of autoproteolysis and substrate hydrolysis.
Biochemistry,
51,
6816-6826.
PubMed id:
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Date:
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18-Mar-14
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Release date:
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26-Mar-14
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Supersedes:
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PROCHECK
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Headers
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References
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Q7L266
(ASGL1_HUMAN) -
Isoaspartyl peptidase/L-asparaginase from Homo sapiens
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Seq:
Struc:
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308 a.a.
295 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Enzyme class 1:
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E.C.3.4.19.5
- beta-aspartyl-peptidase.
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Reaction:
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Cleavage of a beta-linked aspartic residue from the N-terminus of a polypeptide.
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Enzyme class 2:
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E.C.3.5.1.1
- asparaginase.
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Reaction:
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L-asparagine + H2O = L-aspartate + NH4+
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L-asparagine
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+
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H2O
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=
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L-aspartate
Bound ligand (Het Group name = )
corresponds exactly
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+
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NH4(+)
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Biochemistry
51:6816-6826
(2012)
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PubMed id:
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Structures of apo and product-bound human L-asparaginase: insights into the mechanism of autoproteolysis and substrate hydrolysis.
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J.Nomme,
Y.Su,
M.Konrad,
A.Lavie.
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ABSTRACT
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