1QPO

Quinolinate Phosphoribosyl Transferase (QAPRTase) Apo-Enzyme from Mycobacterium Tuberculosis


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.242 
  • R-Value Work: 0.176 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal structure of quinolinic acid phosphoribosyltransferase from Mycobacterium tuberculosis: a potential TB drug target.

Sharma, V.Grubmeyer, C.Sacchettini, J.C.

(1998) Structure 6: 1587-1599

  • DOI: https://doi.org/10.1016/s0969-2126(98)00156-7
  • Primary Citation of Related Structures:  
    1QPN, 1QPO, 1QPQ, 1QPR

  • PubMed Abstract: 

    . Mycobacterium tuberculosis is the single most deadly human pathogen and is responsible for nearly three million deaths every year. Recent elucidation of the mode of action of isoniazid, a frontline antimycobacterial drug, suggests that NAD metabolism is extremely critical for this microorganism. M. tuberculosis depends solely on the de novo pathway to meet its NAD demand. Quinolinic acid phosphoribosyltransferase (QAPRTase), a key enzyme in the de novo biosynthesis of NAD, provides an attractive target for designing novel antitubercular drugs.


  • Organizational Affiliation

    Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
QUINOLINATE ACID PHOSPHORIBOSYL TRANSFERASE
A, B, C, D, E
A, B, C, D, E, F
284Mycobacterium tuberculosis H37RvMutation(s): 0 
Gene Names: NADC
EC: 2.4.2.19
UniProt
Find proteins for P9WJJ7 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
Explore P9WJJ7 
Go to UniProtKB:  P9WJJ7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP9WJJ7
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.242 
  • R-Value Work: 0.176 
  • Space Group: P 31
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 100.584α = 90
b = 100.584β = 90
c = 145.448γ = 120
Software Package:
Software NamePurpose
PHASESphasing
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: 1998-11-24
    Type: Initial release
  • Version 1.1: 2007-10-21
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2023-12-27
    Changes: Data collection, Database references, Derived calculations