2YWB

Crystal structure of GMP synthetase from Thermus thermophilus

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.272 
  • R-Value Work: 0.233 
  • R-Value Observed: 0.233 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history. 


Literature

Crystal structure of GMP synthetase from Thermus thermophilus

Baba, S., Kanagawa, M., Yanai, H., Ishii, T., Kuramitsu, S., Yokoyama, S., Sampei, G., Kawai, G.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GMP synthase [glutamine-hydrolyzing]
A, B, C, D
503Thermus thermophilus HB8Mutation(s): 0 
Gene Names: guaA
EC: 6.3.5.2
UniProt
Find proteins for Q5SI28 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8))
Explore Q5SI28 
Go to UniProtKB:  Q5SI28
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5SI28
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.272 
  • R-Value Work: 0.233 
  • R-Value Observed: 0.233 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 140.949α = 90
b = 114.854β = 93.37
c = 160.033γ = 90
Software Package:
Software NamePurpose
CNSrefinement
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
SOLVEphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-10-23
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Derived calculations, Source and taxonomy, Version format compliance
  • Version 1.2: 2024-03-13
    Changes: Data collection, Database references