3M50

Structure of the 14-3-3/PMA2 complex stabilized by Epibestatin


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.324 
  • R-Value Work: 0.255 
  • R-Value Observed: 0.259 

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Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history


Literature

Identification and structure of small-molecule stabilizers of 14-3-3 protein-protein interactions

Rose, R.Erdmann, S.Bovens, S.Wolf, A.Rose, M.Hennig, S.Waldmann, H.Ottmann, C.

(2010) Angew Chem Int Ed Engl 49: 4129-4132


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
14-3-3-like protein C240Nicotiana tabacumMutation(s): 0 
UniProt
Find proteins for P93343 (Nicotiana tabacum)
Explore P93343 
Go to UniProtKB:  P93343
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP93343
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
N.plumbaginifolia H+-translocating ATPase mRNAB [auth P]31Nicotiana plumbaginifoliaMutation(s): 3 
UniProt
Find proteins for Q42932 (Nicotiana plumbaginifolia)
Explore Q42932 
Go to UniProtKB:  Q42932
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ42932
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
EBT
Query on EBT

Download Ideal Coordinates CCD File 
C [auth A]N-[(2R,3R)-3-amino-2-hydroxy-4-phenylbutanoyl]-L-leucine
C16 H24 N2 O4
VGGGPCQERPFHOB-HZSPNIEDSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.324 
  • R-Value Work: 0.255 
  • R-Value Observed: 0.259 
  • Space Group: I 41 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 97.62α = 90
b = 97.62β = 90
c = 217.03γ = 90
Software Package:
Software NamePurpose
XSCALEdata scaling
PHASERphasing
REFMACrefinement
PDB_EXTRACTdata extraction
XDSdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-05-26
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2014-03-05
    Changes: Database references
  • Version 1.3: 2021-11-10
    Changes: Database references, Derived calculations
  • Version 1.4: 2023-11-01
    Changes: Data collection, Refinement description