1IXH

PHOSPHATE-BINDING PROTEIN (PBP) COMPLEXED WITH PHOSPHATE

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 0.98 Å
  • R-Value Free: 0.141 
  • R-Value Observed: 0.114 

wwPDB Validation   3D Report Full Report


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


Literature

A low energy short hydrogen bond in very high resolution structures of protein receptor--phosphate complexes.

Wang, Z., Luecke, H., Yao, N., Quiocho, F.A.

(1997) Nat Struct Biol 4: 519-522

  • DOI: https://doi.org/10.1038/nsb0797-519
  • Primary Citation of Related Structures:  
    1IXG, 1IXH, 1IXI

  • PubMed Abstract: 

    A very short hydrogen bond between an Asp and a phosphate is established in two high resolution structures (0.98 and 1.05 A). A mutant complex that changes the Asp to an Asn, which forms a normal hydrogen bond, has a similar free energy of binding to the wild type complex, suggesting that the contribution of the short hydrogen bond is not extraordinarily strong.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PHOSPHATE-BINDING PROTEIN321Escherichia coliMutation(s): 0 
Gene Names: PHO-S
UniProt
Find proteins for P0AG82 (Escherichia coli (strain K12))
Explore P0AG82 
Go to UniProtKB:  P0AG82
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0AG82
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
PO4
Query on PO4
Download Ideal Coordinates CCD File 
B [auth A]PHOSPHATE ION
O4 P
NBIIXXVUZAFLBC-UHFFFAOYSA-K
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 0.98 Å
  • R-Value Free: 0.141 
  • R-Value Observed: 0.114 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 41.506α = 90
b = 63.379β = 90
c = 122.373γ = 90
Software Package:
Software NamePurpose
SHELXL-96model building
SHELXL-96refinement
DENZOdata reduction
SCALEPACKdata scaling
SHELXL-96phasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-02-04
    Type: Initial release
  • Version 1.1: 2008-03-21
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-08-09
    Changes: Database references, Derived calculations, Other, Refinement description