1FBA

THE CRYSTAL STRUCTURE OF FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM DROSOPHILA MELANOGASTER AT 2.5 ANGSTROMS RESOLUTION


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Observed: 0.179 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

The crystal structure of fructose-1,6-bisphosphate aldolase from Drosophila melanogaster at 2.5 A resolution.

Hester, G.Brenner-Holzach, O.Rossi, F.A.Struck-Donatz, M.Winterhalter, K.H.Smit, J.D.Piontek, K.

(1991) FEBS Lett 292: 237-242

  • DOI: https://doi.org/10.1016/0014-5793(91)80875-4
  • Primary Citation of Related Structures:  
    1FBA

  • PubMed Abstract: 

    The structure of fructose-1,6-bisphosphate aldolase from Drosophila melanogaster has been determined by X-ray diffraction at 2.5 A resolution. The insect enzyme crystallizes in space group P2(1)2(1)2(1) with lattice replacement with rabbit muscle aldolase as a search model has been employed to solve the structure. To improve the initial phases real space averaging, including phase extension from 4.0 to 2.5 A, has been applied. Refinement of the atomic positions by molecular dynamics resulted in a crystallographic R-factor of 0.214. The tertiary structure resembles in most parts that of the vertebrate aldolase from rabbit muscle. Significant differences were found in surface loops and the N- and C-terminal regions of the protein. Here we present the first aldolase structure where the functionally important C-terminal arm is described completely.


  • Organizational Affiliation

    Laboratorium für Biochemie I, Eidgenössische Technische Hochschule Zürich, Switzerland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE
A, B, C, D
361Drosophila melanogasterMutation(s): 0 
EC: 4.1.2.13
UniProt
Find proteins for P07764 (Drosophila melanogaster)
Explore P07764 
Go to UniProtKB:  P07764
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP07764
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Observed: 0.179 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 86.6α = 90
b = 116.8β = 90
c = 151.58γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
PROLSQrefinement
X-PLORrefinement
X-PLORphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1993-10-31
    Type: Initial release
  • Version 1.1: 2008-03-03
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance