1DOH

STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADPH AND 4-NITRO-INDEN-1-ONE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.205 
  • R-Value Observed: 0.205 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Structures of trihydroxynaphthalene reductase-fungicide complexes: implications for structure-based design and catalysis.

Liao, D.Basarab, G.S.Gatenby, A.A.Valent, B.Jordan, D.B.

(2001) Structure 9: 19-28

  • DOI: https://doi.org/10.1016/s0969-2126(00)00548-7
  • Primary Citation of Related Structures:  
    1DOH, 1G0N, 1G0O

  • PubMed Abstract: 

    Trihydroxynaphthalene reductase catalyzes two intermediate steps in the fungal melanin biosynthetic pathway. The enzyme, a typical short-chain dehydrogenase, is the biochemical target of three commercial fungicides. The fungicides bind preferentially to the NADPH form of the enzyme.


  • Organizational Affiliation

    DuPont Central Research and Development Experimental Station, Wilmington, DE 19880, USA. der-ling.liao@usa.dupont.com


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TRIHYDROXYNAPHTHALENE REDUCTASE
A, B
283Pyricularia griseaMutation(s): 3 
EC: 1.1.1.252
UniProt
Find proteins for Q12634 (Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958))
Explore Q12634 
Go to UniProtKB:  Q12634
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ12634
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
NDP
Query on NDP

Download Ideal Coordinates CCD File 
C [auth A],
E [auth B]
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
C21 H30 N7 O17 P3
ACFIXJIJDZMPPO-NNYOXOHSSA-N
NID
Query on NID

Download Ideal Coordinates CCD File 
D [auth A],
F [auth B]
4-NITRO-INDEN-1-ONE
C9 H5 N O3
UUNZJPCKMDLQPO-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
NID Binding MOAD:  1DOH Ki: 2.4 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.205 
  • R-Value Observed: 0.205 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 142.8α = 90
b = 142.8β = 90
c = 72.94γ = 120
Software Package:
Software NamePurpose
AMoREphasing
X-PLORrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-06-06
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2018-04-04
    Changes: Data collection
  • Version 1.4: 2021-11-03
    Changes: Database references, Derived calculations
  • Version 1.5: 2024-02-07
    Changes: Data collection