5Y51

Crystal structure of PytH_H230A


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.330 
  • R-Value Work: 0.269 
  • R-Value Observed: 0.272 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Structure and Catalytic Mechanism of a Novel Pyrethroid Hydrolase from Sphingobium faniae JZ-2

Xu, D.Q.Ran, T.T.He, J.Wang, W.W.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Pyrethroid hydrolase
A, B, C, D, E
A, B, C, D, E, F
288Sphingobium faniaeMutation(s): 1 
Gene Names: pytH
UniProt
Find proteins for D0VUS3 (Sphingobium faniae)
Explore D0VUS3 
Go to UniProtKB:  D0VUS3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupD0VUS3
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.330 
  • R-Value Work: 0.269 
  • R-Value Observed: 0.272 
  • Space Group: P 42 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 168.375α = 90
b = 168.375β = 90
c = 123.858γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
SCALAdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
State's Key Project of Research and Development PlanChina2016YFD0801102

Revision History  (Full details and data files)

  • Version 1.0: 2018-08-08
    Type: Initial release
  • Version 1.1: 2024-03-27
    Changes: Data collection, Database references