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PDBsum entry 3iv2
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Crystal structure of mature apo-cathepsin l c25a mutant
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Structure:
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Cathepsin l1. Chain: a, b. Fragment: mature protein: unp residues 114-333. Synonym: major excreted protein, mep, cathepsin l1 heavy chain and cathepsin l1 light chain. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: ctsl1, ctsl. Expressed in: pichia pastoris. Expression_system_taxid: 4922
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Resolution:
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2.20Å
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R-factor:
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0.204
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R-free:
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0.244
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Authors:
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M.A.Adams-Cioaba,J.C.Krupa,J.S.Mort,C.Bountra,J.Weigelt, C.H.Arrowsmith,A.M.Edwards,A.Bochkarev,J.Min
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Key ref:
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M.A.Adams-Cioaba
et al.
(2011).
Structural basis for the recognition and cleavage of histone H3 by cathepsin L.
Nat Commun,
2,
197-197.
PubMed id:
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Date:
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31-Aug-09
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Release date:
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23-Mar-10
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PROCHECK
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Headers
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References
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P07711
(CATL1_HUMAN) -
Procathepsin L from Homo sapiens
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Seq: Struc:
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333 a.a.
219 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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E.C.3.4.22.15
- cathepsin L.
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Reaction:
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Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity towards protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.
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Nat Commun
2:197-197
(2011)
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PubMed id:
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Structural basis for the recognition and cleavage of histone H3 by cathepsin L.
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M.A.Adams-Cioaba,
J.C.Krupa,
C.Xu,
J.S.Mort,
J.Min.
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ABSTRACT
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');
}
}
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