1WE0

Crystal structure of peroxiredoxin (AhpC) from Amphibacillus xylanus

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.235 
  • R-Value Work: 0.208 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history. 


Literature

Crystal structure of decameric peroxiredoxin (AhpC) from Amphibacillus xylanus

Kitano, K., Kita, A., Hakoshima, T., Niimura, Y., Miki, K.

(2005) Proteins 59: 644-647


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
alkyl hydroperoxide reductase C
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J
187Amphibacillus xylanusMutation(s): 0 
EC: 1.11.1
UniProt
Find proteins for K0J4Q8 (Amphibacillus xylanus (strain ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667 / NBRC 15112 / Ep01))
Explore K0J4Q8 
Go to UniProtKB:  K0J4Q8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupK0J4Q8
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
NH4
Query on NH4
Download Ideal Coordinates CCD File 
K [auth F],
L [auth J]		AMMONIUM ION
H4 N
QGZKDVFQNNGYKY-UHFFFAOYSA-O
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.235 
  • R-Value Work: 0.208 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 79.216α = 77.22
b = 79.319β = 82.33
c = 104.449γ = 80.08
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
CNSrefinement
CNSphasing

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-03-29
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2018-02-07
    Changes: Experimental preparation