3IL0

The crystal structure of the aminopeptidase P,XAA-pro aminopeptidase from Streptococcus thermophilus


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.237 
  • R-Value Work: 0.201 
  • R-Value Observed: 0.203 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

The crystal structure of the aminopeptidase P,XAA-pro aminopeptidase from Streptococcus thermophilus

Zhang, R.Hatzos, C.Cobb, G.Joachimiak, A.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Aminopeptidase P; XAA-pro aminopeptidase
A, B
131Streptococcus thermophilus LMG 18311Mutation(s): 0 
Gene Names: GI:55737699pepPstu1742
UniProt
Find proteins for Q5M2R3 (Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311))
Explore Q5M2R3 
Go to UniProtKB:  Q5M2R3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5M2R3
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.237 
  • R-Value Work: 0.201 
  • R-Value Observed: 0.203 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 43.303α = 90
b = 80.396β = 90
c = 100.858γ = 90
Software Package:
Software NamePurpose
SBC-Collectdata collection
HKL-3000phasing
REFMACrefinement
HKL-3000data reduction
HKL-3000data scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-09-08
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Source and taxonomy, Version format compliance
  • Version 1.2: 2024-02-21
    Changes: Data collection, Database references, Derived calculations