1HKA

6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Observed: 0.182 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Crystal structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, a potential target for the development of novel antimicrobial agents.

Xiao, B.Shi, G.Chen, X.Yan, H.Ji, X.

(1999) Structure 7: 489-496

  • DOI: https://doi.org/10.1016/s0969-2126(99)80065-3
  • Primary Citation of Related Structures:  
    1HKA

  • PubMed Abstract: 

    Folate cofactors are essential for life. Mammals derive folates from their diet, whereas most microorganisms must synthesize folates de novo. Enzymes of the folate pathway therefore provide ideal targets for the development of antimicrobial agents. 6-Hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) catalyzes the transfer of pyrophosphate from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP), the first reaction in the folate biosynthetic pathway.


  • Organizational Affiliation

    ABL-Basic Research Program, NCI-Frederick Cancer Research and Development Center, MD 21702, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE158Escherichia coliMutation(s): 0 
Gene Names: FOLK
EC: 2.7.6.3
UniProt
Find proteins for P26281 (Escherichia coli (strain K12))
Explore P26281 
Go to UniProtKB:  P26281
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP26281
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Observed: 0.182 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 36.32α = 90
b = 51.98β = 110.12
c = 41.49γ = 90
Software Package:
Software NamePurpose
PHASESphasing
SHELXL-97refinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-06-08
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-09-13
    Changes: Refinement description
  • Version 1.4: 2023-08-30
    Changes: Data collection, Database references, Structure summary