PDBsum entry: 1au2

Hydrolase

PDB id: 1au2

Contents

Protein chain

215 a.a. *

Ligands

POS

Waters ×62

* Residue conservation analysis

PDB id:

1au2

Name:

Hydrolase

Title:

Crystal structure of the cysteine protease human cathepsin k in complex with a covalent propanone 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: sf9. Cell: osteoclast. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9.

Resolution:

2.60Å R-factor: 0.240 R-free: 0.333

Authors:

B.Zhao,W.W.Smith,C.A.Janson,S.S.Abdel-Meguid

Key ref:

D.S.Yamashita et al. (1997). Structure and design of potent and selective cathepsin k inhibitors. J.Am.Chem.Soc., 119, PubMed id: -1

Date:

10-Sep-97 Release date: 14-Oct-98

Protein chain

P43235  (CATK_HUMAN) -  Cathepsin K

Seq: 329 a.a.

Struc: 215 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.22.38 - Cathepsin K.
• 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.

 Gene Ontology (GO) functional annotation 

• Biological process: proteolysis (1 term)
• Biochemical function: cysteine-type peptidase activity (2 terms)