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PDBsum entry 1bgo

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Hydrolase PDB id
1bgo

 

 

 

 

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Contents
Protein chain
215 a.a. *
Ligands
I10
Waters ×19
* Residue conservation analysis
PDB id:
1bgo
Name: Hydrolase
Title: Crystal structure of cysteine protease human cathepsin k in complex with a covalent peptidomimetic inhibitor
Structure: Cathepsin k. Chain: a. Engineered: yes. Other_details: inhibitor covalently bound to active site cys 25
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell_line: sf21. Cell: osteoclast. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf21.
Resolution:
2.30Å     R-factor:   0.240     R-free:   0.296
Authors: R.L.Desjarlais,D.S.Yamashita,H.-J.Oh,W.E.Bondinell,I.N.Uzinskas, K.F.Erhard,A.C.Allen,R.C.Haltiwanger,B.Zhao,W.W.Smith,S.S.Abdel- Meguid,K.D'Alessio,C.A.Janson,M.S.Mcqueney,T.A.Tomaszek,M.A.Levy, D.F.Veber
Key ref: R.L.Desjarlais et al. (1998). Use of X-Ray co-Crystal structures and molecular modeling to design potent and selective non-Peptide inhibitors of cathepsin k. J am chem soc, 120, 9114.
Date:
29-May-98     Release date:   08-Jun-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P43235  (CATK_HUMAN) -  Cathepsin K from Homo sapiens
Seq:
Struc:
329 a.a.
215 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.22.38  - cathepsin K.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Broad proteolytic activity. With small-molecule substrates and inhibitors, the major determinant of specificity is P2, which is preferably Leu, Met > Phe, and not Arg.

 

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