1AU3

CRYSTAL STRUCTURE OF THE CYSTEINE PROTEASE HUMAN CATHEPSIN K IN COMPLEX WITH A COVALENT PYRROLIDINONE INHIBITOR

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.353 
  • R-Value Work: 0.193 
  • R-Value Observed: 0.193 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history. 


Literature

Conformationally constrained 1,3-diamino ketones: a series of potent inhibitors of the cysteine protease cathepsin K.

Marquis, R.W., Yamashita, D.S., Ru, Y., LoCastro, S.M., Oh, H.J., Erhard, K.F., DesJarlais, R.L., Head, M.S., Smith, W.W., Zhao, B., Janson, C.A., Abdel-Meguid, S.S., Tomaszek, T.A., Levy, M.A., Veber, D.F.

(1998) J Med Chem 41: 3563-3567


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CATHEPSIN K215Homo sapiensMutation(s): 0 
EC: 3.4.22.38
UniProt & NIH Common Fund Data Resources
Find proteins for P43235 (Homo sapiens)
Explore P43235 
Go to UniProtKB:  P43235
PHAROS:  P43235
GTEx:  ENSG00000143387 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP43235
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
PCM
Query on PCM
Download Ideal Coordinates CCD File 
B [auth A]1-[N[(PHENYLMETHOXY)CARBONYL]-L-LEUCYL-4-[[N/N-[(PHENYLMETHOXY)CARBONYL]-/NL-LEUCYL]AMINO]-3-PYRROLIDINONE/N
C32 H42 N4 O7
GXENQLUSOCKXDN-GMQQYTKMSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.353 
  • R-Value Work: 0.193 
  • R-Value Observed: 0.193 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 38.84α = 90
b = 50.99β = 90
c = 103.58γ = 90
Software Package:
Software NamePurpose
XENGENdata collection
XENGENdata reduction
X-PLORmodel building
X-PLORrefinement
XENGENdata scaling
X-PLORphasing

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-10-14
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-03-07
    Changes: Data collection, Other
  • Version 1.4: 2023-08-02
    Changes: Database references, Derived calculations, Refinement description