1LYV

High-resolution structure of the catalytically inactive yersinia tyrosine phosphatase C403A mutant in complex with phosphate.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.36 Å
  • R-Value Free: 0.190 
  • R-Value Observed: 0.129 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

High-resolution structure of the catalytically inactive yersinia tyrosine phosphatase C403A mutant in complex with phosphate.

Evdokimov, A.G.Waugh, D.S.Routzahn, K.Tropea, J.Cherry, S.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN-TYROSINE PHOSPHATASE YOPH306Yersinia enterocoliticaMutation(s): 3 
Gene Names: YopH
EC: 3.1.3.48
UniProt
Find proteins for P15273 (Yersinia enterocolitica)
Explore P15273 
Go to UniProtKB:  P15273
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP15273
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.36 Å
  • R-Value Free: 0.190 
  • R-Value Observed: 0.129 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 55.456α = 90
b = 49.331β = 90
c = 97.537γ = 90
Software Package:
Software NamePurpose
SHELXL-97refinement
HKL-2000data reduction
SCALEPACKdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-07-03
    Type: Initial release
  • Version 1.1: 2008-04-28
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-10-11
    Changes: Refinement description
  • Version 1.4: 2021-10-27
    Changes: Database references, Derived calculations
  • Version 1.5: 2024-02-14
    Changes: Data collection, Refinement description