1OGW

Synthetic Ubiquitin with fluoro-Leu at 50 and 67

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.32 Å
  • R-Value Observed: 0.222 

Starting Model: experimental
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wwPDB Validation   3D Report Full Report


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


Literature

Synthesis, Structural and Biological Studies of Ubiquitin Mutants Containing (2S, 4S)-5-Fluoroleucine Residues Strategically Placed in the Hydrophobic Core

Alexeev, D., Barlow, P.N., Bury, S.M., Charrier, J.-D., Cooper, A., Hadfield, D., Jamieson, C., Kelly, S.M., Layfield, R., Mayer, R.J., Mcsparran, H., Price, N.C., Ramage, R., Sawyer, L., Starkmann, B.A., Uhrin, D., Willken, J., Young, D.W.

(2003) Chembiochem 4: 894


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
UBIQUITIN76Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P0CG48 (Homo sapiens)
Explore P0CG48 
Go to UniProtKB:  P0CG48
PHAROS:  P0CG48
GTEx:  ENSG00000150991 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0CG48
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
LEF
Query on LEF
A
L-PEPTIDE LINKINGC6 H12 F N O2LEU
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.32 Å
  • R-Value Observed: 0.222 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 50.84α = 90
b = 42.77β = 90
c = 28.95γ = 90
Software Package:
Software NamePurpose
SHELXL-97refinement
DENZOdata reduction
SCALEPACKdata scaling
SHELXL-97phasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2003-05-30
    Type: Initial release
  • Version 1.1: 2011-12-07
    Changes: Database references, Derived calculations, Other, Refinement description, Structure summary, Version format compliance
  • Version 1.2: 2023-12-13
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description
  • Version 1.3: 2024-11-13
    Changes: Structure summary