1STD

CRYSTAL STRUCTURE OF SCYTALONE DEHYDRATASE: A DISEASE DETERMINANT OF THE RICE PATHOGEN, MAGNAPORTHE GRISEA


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Work: 0.179 
  • R-Value Observed: 0.179 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal structure of scytalone dehydratase--a disease determinant of the rice pathogen, Magnaporthe grisea.

Lundqvist, T.Rice, J.Hodge, C.N.Basarab, G.S.Pierce, J.Lindqvist, Y.

(1994) Structure 2: 937-944

  • DOI: https://doi.org/10.1016/s0969-2126(94)00095-6
  • Primary Citation of Related Structures:  
    1STD

  • PubMed Abstract: 

    Rice blast is caused by the pathogenic fungus,-Magnaporthe grisea. Non-pathogenic mutants have been identified that lack enzymes in the biosynthetic pathway of dihydroxynapthalene-derived melanin. These enzymes are therefore prime targets for fungicides designed to control rice blast disease. One of the enzymes identified by genetic analysis as a disease determinant is scytalone dehydratase.


  • Organizational Affiliation

    Department of Molecular Biology, Swedish University of Agricultural Sciences Uppsala Biomedical Center.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SCYTALONE DEHYDRATASE172Pyricularia griseaMutation(s): 0 
EC: 4.2.1.94
UniProt
Find proteins for P56221 (Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958))
Explore P56221 
Go to UniProtKB:  P56221
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP56221
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
BFS
Query on BFS

Download Ideal Coordinates CCD File 
C [auth A]N-[1-(4-BROMOPHENYL)ETHYL]-5-FLUORO SALICYLAMIDE
C15 H13 Br F N O2
KFTNEILVDDUXGR-SECBINFHSA-N
SO4
Query on SO4

Download Ideal Coordinates CCD File 
B [auth A]SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
Binding Affinity Annotations 
IDSourceBinding Affinity
BFS PDBBind:  1STD Ki: 0.05 (nM) from 1 assay(s)
BindingDB:  1STD Ki: min: 46, max: 47 (nM) from 2 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Work: 0.179 
  • R-Value Observed: 0.179 
  • Space Group: P 3 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 75.5α = 90
b = 75.5β = 90
c = 73.8γ = 120
Software Package:
Software NamePurpose
X-PLORmodel building
X-PLORrefinement
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1995-08-19
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references, Derived calculations, Other