1FR3

THE HIGH RESOLUTION STRUCTURE OF A MOLYBDATE BINDING PROTEIN FROM SPOROMUSA OVATA

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Free: 0.198 
  • R-Value Work: 0.185 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history. 


Literature

Structure of the molybdate/tungstate binding protein mop from Sporomusa ovata.

Wagner, U.G., Stupperich, E., Kratky, C.

(2000) Structure 8: 1127-1136

  • DOI: https://doi.org/10.1016/s0969-2126(00)00525-6
  • Primary Citation of Related Structures:  
    1FR3

  • PubMed Abstract: 

    Transport of molybdenum into bacteria involves a high-affinity ABC transporter system whose expression is controlled by a repressor protein called ModE. While molybdate transport is tightly coupled to utilization in some bacteria, other organisms have molybdenum storage proteins. One class of putative molybdate storage proteins is characterized by a sequence consisting of about 70 amino acids (Mop). A tandem repeat of Mop sequences also constitutes the molybdate binding domain of ModE.

    • Organizational Affiliation: 

    Institut für Chemie Strukturbiologie Karl-Franzens-Universität A-8010, Graz, Austria.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MOLYBDATE/TUNGSTATE BINDING PROTEIN
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J, K, L
67Sporomusa ovataMutation(s): 0 
UniProt
Find proteins for Q7SIF7 (Sporomusa ovata)
Explore Q7SIF7 
Go to UniProtKB:  Q7SIF7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ7SIF7
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
WO4
Query on WO4
Download Ideal Coordinates CCD File 
AA [auth L]
BA [auth L]
M [auth A]
N [auth A]
O [auth B]
AA [auth L],
BA [auth L],
M [auth A],
N [auth A],
O [auth B],
P [auth B],
Q [auth C],
R [auth D],
S [auth E],
T [auth F],
U [auth G],
V [auth G],
W [auth H],
X [auth I],
Y [auth J],
Z [auth K]
TUNGSTATE(VI)ION
O4 W
PBYZMCDFOULPGH-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Free: 0.198 
  • R-Value Work: 0.185 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 109.724α = 90
b = 138.328β = 90
c = 110.368γ = 90
Software Package:
Software NamePurpose
CNSrefinement
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
CNSphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-12-06
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-07
    Changes: Data collection, Database references, Derived calculations