3KCI

The third RLD domain of HERC2

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.195 
  • R-Value Work: 0.152 
  • R-Value Observed: 0.154 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history. 


Literature

Structure of the Third RLD Domain of Herc2

Walker, J.R., Qiu, L., Vesterberg, A., Weigelt, J., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Bochkarev, A., Dhe-Paganon, S.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Probable E3 ubiquitin-protein ligase HERC2389Homo sapiensMutation(s): 0 
Gene Names: D15F37S1, DKFZP547P028, HERC2
EC: 6.3.2
UniProt & NIH Common Fund Data Resources
Find proteins for O95714 (Homo sapiens)
Explore O95714 
Go to UniProtKB:  O95714
PHAROS:  O95714
GTEx:  ENSG00000128731 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO95714
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.195 
  • R-Value Work: 0.152 
  • R-Value Observed: 0.154 
  • Space Group: P 61
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 52.673α = 90
b = 52.673β = 90
c = 215.242γ = 120
Software Package:
Software NamePurpose
HKL-2000data collection
PHASERphasing
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-11-03
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-09-06
    Changes: Data collection, Database references, Refinement description