6HP1

Crystal Structure of the O-Methyltransferase from the trans-AT PKS multienzyme C0ZGQ3 of Brevibacillus brevis


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.204 
  • R-Value Work: 0.173 
  • R-Value Observed: 0.175 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

Structural and Functional Analysis of an O-Methyltransferase from the trans-AT PKS biosynthesis pathway

Jakob, R.P.Felber, P.Demyanenko, Y.Delbart, F.Maier, T.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Putative polyketide synthase344Brevibacillus brevis NBRC 100599Mutation(s): 0 
Gene Names: BBR47_39850
UniProt
Find proteins for C0ZGQ3 (Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599))
Explore C0ZGQ3 
Go to UniProtKB:  C0ZGQ3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupC0ZGQ3
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.204 
  • R-Value Work: 0.173 
  • R-Value Observed: 0.175 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 44.613α = 90
b = 71.76β = 104.07
c = 61.192γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2019-10-09
    Type: Initial release