3ET6

The crystal structure of the catalytic domain of a eukaryotic guanylate cyclase


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.55 Å
  • R-Value Free: 0.215 
  • R-Value Work: 0.172 
  • R-Value Observed: 0.174 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

The crystal structure of the catalytic domain of a eukaryotic guanylate cyclase.

Winger, J.A.Derbyshire, E.R.Lamers, M.H.Marletta, M.A.Kuriyan, J.

(2008) BMC Struct Biol 8: 42-42

  • DOI: https://doi.org/10.1186/1472-6807-8-42
  • Primary Citation of Related Structures:  
    3ET6

  • PubMed Abstract: 

    Soluble guanylate cyclases generate cyclic GMP when bound to nitric oxide, thereby linking nitric oxide levels to the control of processes such as vascular homeostasis and neurotransmission. The guanylate cyclase catalytic module, for which no structure has been determined at present, is a class III nucleotide cyclase domain that is also found in mammalian membrane-bound guanylate and adenylate cyclases.


  • Organizational Affiliation

    Department of Molecular and Cell Biology, University of California, Berkeley, CA, USA. wingerj@berkeley.edu


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Soluble guanylyl cyclase beta190Chlamydomonas reinhardtiiMutation(s): 0 
Gene Names: CHLREDRAFT_187517CYG12
UniProt
Find proteins for Q5YLC2 (Chlamydomonas reinhardtii)
Explore Q5YLC2 
Go to UniProtKB:  Q5YLC2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5YLC2
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Soluble guanylyl cyclase beta190Chlamydomonas reinhardtiiMutation(s): 0 
Gene Names: CHLREDRAFT_187517CYG12
UniProt
Find proteins for Q5YLC2 (Chlamydomonas reinhardtii)
Explore Q5YLC2 
Go to UniProtKB:  Q5YLC2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5YLC2
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.55 Å
  • R-Value Free: 0.215 
  • R-Value Work: 0.172 
  • R-Value Observed: 0.174 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 123.678α = 90
b = 123.678β = 90
c = 62.822γ = 120
Software Package:
Software NamePurpose
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACTdata extraction
BOSdata collection

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-10-14
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-09-06
    Changes: Data collection, Database references, Derived calculations, Refinement description