2YYS

Crystal structure of the proline iminopeptidase-related protein TTHA1809 from Thermus thermophilus HB8

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.208 
  • R-Value Work: 0.177 
  • R-Value Observed: 0.178 

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


Literature

Crystal structure of the proline iminopeptidase-related protein TTHA1809 from Thermus thermophilus HB8

Okai, M., Miyauchi, Y., Ebihara, A., Lee, W.C., Nagata, K., Tanokura, M.

(2008) Proteins 70: 1646-1649


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Proline iminopeptidase-related protein
A, B
286Thermus thermophilus HB8Mutation(s): 0 
UniProt
Find proteins for Q5SHC1 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8))
Explore Q5SHC1 
Go to UniProtKB:  Q5SHC1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5SHC1
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.208 
  • R-Value Work: 0.177 
  • R-Value Observed: 0.178 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 126.93α = 90
b = 126.93β = 90
c = 114.295γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
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: 2008-02-26
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Source and taxonomy, Version format compliance
  • Version 1.2: 2024-03-13
    Changes: Data collection, Database references, Derived calculations