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PDBsum entry 3k24

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3k24
Jmol
Contents
Protein chains
220 a.a. *
Ligands
GLN-LEU-ALA ×2
NAG
NAG-NDG-MAN-MAN-
BMA-NDG
Waters ×32
* Residue conservation analysis
PDB id:
3k24
Name: Hydrolase
Title: Crystal structure of mature apo-cathepsin l c25a mutant in c with gln-leu-ala peptide
Structure: Cathepsin l1. Chain: a, b. Fragment: mc25a: unp residues 114-333. Synonym: major excreted protein, mep, cathepsin l1 heavy ch cathepsin l1 light chain. Engineered: yes. Mutation: yes. H3 peptide. Chain: c, d.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ctsl1, ctsl. Expressed in: pichia pastoris. Expression_system_taxid: 4922. Synthetic: yes. Other_details: synthetic peptide
Resolution:
2.50Å     R-factor:   0.212     R-free:   0.270
Authors: M.A.Adams-Cioaba,J.C.Krupa,J.S.Mort,C.Bountra,J.Weigelt, C.H.Arrowsmith,A.M.Edwards,A.Bochkarev,J.Min,Structural Gen Consortium (Sgc)
Key ref: 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: 21326229
Date:
29-Sep-09     Release date:   23-Mar-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P07711  (CATL1_HUMAN) -  Cathepsin L1
Seq:
Struc:
333 a.a.
220 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.4.22.15  - Cathepsin L.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 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.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     proteolysis   1 term 
  Biochemical function     cysteine-type peptidase activity     1 term  

 

 
Nat Commun 2:197-197 (2011)
PubMed id: 21326229  
 
 
Structural basis for the recognition and cleavage of histone H3 by cathepsin L.
M.A.Adams-Cioaba, J.C.Krupa, C.Xu, J.S.Mort, J.Min.
 
  ABSTRACT  
 
No abstract given.