5C2J

Complex structure of the GAP domain of MgcRacGAP and Cdc42


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.263 
  • R-Value Work: 0.198 
  • R-Value Observed: 0.198 

Starting Models: experimental
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wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Structural basis of G-protein target alternation of MgcRacGAP by phospholylation

Murayama, K.Kato-Murayama, M.Hosaka, T.Kawashima, T.Kitamura, T.Yokoyama, S.Shirouzu, M.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Rac GTPase-activating protein 1208Homo sapiensMutation(s): 0 
Gene Names: RACGAP1KIAA1478MGCRACGAP
UniProt & NIH Common Fund Data Resources
Find proteins for Q9H0H5 (Homo sapiens)
Explore Q9H0H5 
Go to UniProtKB:  Q9H0H5
PHAROS:  Q9H0H5
GTEx:  ENSG00000161800 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9H0H5
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Cell division control protein 42 homolog198Mus musculusMutation(s): 0 
Gene Names: Cdc42
EC: 3.6.5.2
UniProt & NIH Common Fund Data Resources
Find proteins for P60766 (Mus musculus)
Explore P60766 
Go to UniProtKB:  P60766
IMPC:  MGI:106211
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP60766
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.263 
  • R-Value Work: 0.198 
  • R-Value Observed: 0.198 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 43.324α = 90
b = 74.237β = 96.67
c = 55.423γ = 90
Software Package:
Software NamePurpose
CNSrefinement
HKL-2000data reduction
HKL-2000data scaling
MOLREPphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-06-22
    Type: Initial release
  • Version 1.1: 2020-02-19
    Changes: Data collection, Derived calculations
  • Version 1.2: 2023-11-08
    Changes: Data collection, Database references, Refinement description
  • Version 1.3: 2024-11-20
    Changes: Structure summary