4KNG

Crystal structure of human LGR5-RSPO1-RNF43


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.276 
  • R-Value Work: 0.232 
  • R-Value Observed: 0.234 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history



Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Leucine-rich repeat-containing G-protein coupled receptor 5
A, B
531Homo sapiensMutation(s): 0 
Gene Names: LGR5GPR49GPR67
UniProt & NIH Common Fund Data Resources
Find proteins for O75473 (Homo sapiens)
Explore O75473 
Go to UniProtKB:  O75473
PHAROS:  O75473
GTEx:  ENSG00000139292 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO75473
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
R-spondin-1C [auth M],
D [auth P]
115Homo sapiensMutation(s): 0 
Gene Names: RSPO1
UniProt & NIH Common Fund Data Resources
Find proteins for Q2MKA7 (Homo sapiens)
Explore Q2MKA7 
Go to UniProtKB:  Q2MKA7
PHAROS:  Q2MKA7
GTEx:  ENSG00000169218 
Entity Groups  
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UniProt GroupQ2MKA7
Sequence Annotations
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
E3 ubiquitin-protein ligase RNF43
E, F
160Homo sapiensMutation(s): 0 
Gene Names: RNF43
EC: 6.3.2
UniProt & NIH Common Fund Data Resources
Find proteins for Q68DV7 (Homo sapiens)
Explore Q68DV7 
Go to UniProtKB:  Q68DV7
PHAROS:  Q68DV7
GTEx:  ENSG00000108375 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ68DV7
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.276 
  • R-Value Work: 0.232 
  • R-Value Observed: 0.234 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 104.575α = 90
b = 120.971β = 90
c = 181.009γ = 90
Software Package:
Software NamePurpose
HKL-3000data collection
X-PLORmodel building
REFMACrefinement
HKL-3000data reduction
SCALAdata scaling
X-PLORphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-06-19
    Type: Initial release
  • Version 1.1: 2013-07-03
    Changes: Data collection
  • Version 1.2: 2013-07-24
    Changes: Database references
  • Version 1.3: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Data collection, Database references, Derived calculations, Structure summary