3WZL

ZEN lactonase

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.266 
  • R-Value Work: 0.210 
  • R-Value Observed: 0.213 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history. 


Literature

Crystal structure and substrate-binding mode of the mycoestrogen-detoxifying lactonase ZHD from Clonostachys rosea

Peng, W., Ko, T.P., Yang, Y., Zheng, Y., Chen, C.C., Zhu, Z., Huang, C.H., Zeng, Y.F., Huang, J.W., Wand, A.H.-J., Liu, J.R., Guo, R.T.

(2014) RSC Adv 4: 62321-62325


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Zearalenone hydrolase
A, B, C
278Clonostachys roseaMutation(s): 0 
Gene Names: zhd101
UniProt
Find proteins for Q8NKB0 (Bionectria ochroleuca)
Explore Q8NKB0 
Go to UniProtKB:  Q8NKB0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8NKB0
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.266 
  • R-Value Work: 0.210 
  • R-Value Observed: 0.213 
  • Space Group: P 61 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 86.637α = 90
b = 86.637β = 90
c = 474.016γ = 120
Software Package:
Software NamePurpose
Blu-Icedata collection
SOLVEphasing
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-11-26
    Type: Initial release
  • Version 1.1: 2017-11-22
    Changes: Refinement description
  • Version 1.2: 2024-03-20
    Changes: Data collection, Database references, Refinement description