1FTN

CRYSTAL STRUCTURE OF THE HUMAN RHOA/GDP COMPLEX


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.304 
  • R-Value Work: 0.186 

Starting Model: experimental
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wwPDB Validation   3D Report Full Report


This is version 1.6 of the entry. See complete history


Literature

Crystal structure of RhoA-GDP and its functional implications.

Wei, Y.Zhang, Y.Derewenda, U.Liu, X.Minor, W.Nakamoto, R.K.Somlyo, A.V.Somlyo, A.P.Derewenda, Z.S.

(1997) Nat Struct Biol 4: 699-703

  • DOI: https://doi.org/10.1038/nsb0997-699
  • Primary Citation of Related Structures:  
    1FTN

  • PubMed Abstract: 

    RhoA, a ubiquitous intracellular GTPase, mediates cytoskeletal responses to extracellular signals. A 2.1 A resolution crystal structure of the human RhoA-GDP complex shows unique stereochemistry in the switch I region, which results in a novel mode of Mg2+ binding.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TRANSFORMING PROTEIN RHOA (H12)193Homo sapiensMutation(s): 1 
Gene Names: SYNTHETIC HUMAN RHOA GENE
EC: 3.6.5.2
UniProt & NIH Common Fund Data Resources
Find proteins for P61586 (Homo sapiens)
Explore P61586 
Go to UniProtKB:  P61586
PHAROS:  P61586
GTEx:  ENSG00000067560 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP61586
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
GDP
Query on GDP

Download Ideal Coordinates CCD File 
C [auth A]GUANOSINE-5'-DIPHOSPHATE
C10 H15 N5 O11 P2
QGWNDRXFNXRZMB-UUOKFMHZSA-N
MG
Query on MG

Download Ideal Coordinates CCD File 
B [auth A]MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.304 
  • R-Value Work: 0.186 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 31.92α = 90
b = 65.96β = 90
c = 83.37γ = 90
Software Package:
Software NamePurpose
AMoREphasing
MLPHAREphasing
SHELX-90model building
SHELX-90refinement
DENZOdata reduction
SCALEPACKdata scaling
SHELX-90phasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-03-18
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2021-11-03
    Changes: Data collection, Database references, Derived calculations
  • Version 1.4: 2022-04-13
    Changes: Database references, Structure summary
  • Version 1.5: 2024-02-07
    Changes: Data collection
  • Version 1.6: 2024-04-03
    Changes: Refinement description