2C46

CRYSTAL STRUCTURE OF THE HUMAN RNA guanylyltransferase and 5'- phosphatase


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.234 
  • R-Value Work: 0.204 
  • R-Value Observed: 0.206 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Crystal Structure of the Human RNA Guanylyltransferase and 5'-Phosphatase

Debreczeni, J.Johansson, C.Longman, E.Gileadi, O.Savitskysmee, P.Smee, C.Bunkoczi, G.Ugochukwu, E.von Delft, F.Sundstrom, M.Weigelt, J.Arrowsmith, C.Edwards, A.Knapp, S.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MRNA CAPPING ENZYME
A, B, C, D
241Homo sapiensMutation(s): 0 
EC: 2.7.7.50
UniProt & NIH Common Fund Data Resources
Find proteins for O60942 (Homo sapiens)
Explore O60942 
Go to UniProtKB:  O60942
PHAROS:  O60942
GTEx:  ENSG00000111880 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO60942
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.234 
  • R-Value Work: 0.204 
  • R-Value Observed: 0.206 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 60.4α = 90
b = 161.6β = 104.7
c = 60.7γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2005-11-01
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.2: 2012-12-05
    Changes: Database references, Structure summary
  • Version 1.3: 2018-01-24
    Changes: Database references
  • Version 1.4: 2023-12-13
    Changes: Data collection, Database references, Other, Refinement description