1ATG

AZOTOBACTER VINELANDII PERIPLASMIC MOLYBDATE-BINDING PROTEIN

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.20 Å
  • R-Value Free: 0.183 
  • R-Value Work: 0.164 

wwPDB Validation   3D Report Full Report


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


Literature

Ligand size is a major determinant of specificity in periplasmic oxyanion-binding proteins: the 1.2 A resolution crystal structure of Azotobacter vinelandii ModA.

Lawson, D.M., Williams, C.E., Mitchenall, L.A., Pau, R.N.

(1998) Structure 6: 1529-1539

  • DOI: https://doi.org/10.1016/s0969-2126(98)00151-8
  • Primary Citation of Related Structures:  
    1ATG

  • PubMed Abstract: 

    . Periplasmic receptors constitute a diverse class of binding proteins that differ widely in size, sequence and ligand specificity. Nevertheless, almost all of them display a common beta/alpha folding motif and have similar tertiary structures consisting of two globular domains. The ligand is bound at the bottom of a deep cleft, which lies at the interface between these two domains. The oxyanion-binding proteins are notable in that they can discriminate between very similar ligands.

    • Organizational Affiliation: 

    Nitrogen Fixation Laboratory John Innes Centre Norwich NR4 7UH UK. david.lawson@bbsrc.ac.uk


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PERIPLASMIC MOLYBDATE-BINDING PROTEIN231Azotobacter vinelandiiMutation(s): 0 
UniProt
Find proteins for Q7SIH2 (Azotobacter vinelandii)
Explore Q7SIH2 
Go to UniProtKB:  Q7SIH2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ7SIH2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.20 Å
  • R-Value Free: 0.183 
  • R-Value Work: 0.164 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 32.934α = 90
b = 88.802β = 93.55
c = 41.746γ = 90
Software Package:
Software NamePurpose
VARIOUSmodel building
DMmodel building
Omodel building
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
CCP4phasing
DMphasing
OTHERS)phasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-10-14
    Type: Initial release
  • Version 1.1: 2008-03-03
    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