4QEB

Dcps in complex with covalent inhibitor targeting Tyrosine


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.21 Å
  • R-Value Free: 0.276 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.214 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Human Dcps in complex with covalent inhibitor

Liu, S.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
m7GpppX diphosphatase
A, B, C, D
337Homo sapiensMutation(s): 0 
Gene Names: DCPSDCS1HINT5HSPC015
EC: 3.6.1.59
UniProt & NIH Common Fund Data Resources
Find proteins for Q96C86 (Homo sapiens)
Explore Q96C86 
Go to UniProtKB:  Q96C86
PHAROS:  Q96C86
GTEx:  ENSG00000110063 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ96C86
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.21 Å
  • R-Value Free: 0.276 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.214 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 101.25α = 90
b = 105.23β = 90
c = 139.96γ = 90
Software Package:
Software NamePurpose
Jdirectdata collection
MOLREPphasing
BUSTERrefinement
autoPROCdata scaling
CCP4data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

  • Released Date: 2015-05-20 
  • Deposition Author(s): Liu, S.

Revision History  (Full details and data files)

  • Version 1.0: 2015-05-20
    Type: Initial release
  • Version 1.1: 2023-09-20
    Changes: Data collection, Database references, Derived calculations, Refinement description