1WAE

Crystal structure of H129V Mutant of Alcaligenes Xylosoxidans Nitrite Reductase

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.226 
  • R-Value Work: 0.201 
  • R-Value Observed: 0.202 

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


Literature

Observation of an Unprecedented Cu Bis-His Site: Crystal Structure of the H129V Mutant of Nitrite Reductase

Ellis, M.J., Antonyuk, S.V., Strange, R.W., Sawers, G., Eady, R.R., Hasnain, S.S.

(2004) Inorg Chem 43: 7591

  • DOI: https://doi.org/10.1021/ic048966p
  • Primary Citation of Related Structures:  
    1WAE

  • PubMed Abstract: 

    Copper nitrite reductases contain both an electron-transfer type 1 Cu site and a catalytic type 2 Cu site. We have mutated one of the type 2 copper ligating histidines to observe the effect on catalytic turnover. This mutation has created a unique site where Cu is ligated by 2 His Nepsilon2 atoms alone.

    • Organizational Affiliation: 

    Molecular Biophysics Group, CCLRC Daresbury Laboratory, Warrington, Cheshire, UK.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
DISSIMILATORY COPPER-CONTAINING NITRITE REDUCTASE336Achromobacter xylosoxidansMutation(s): 1 
EC: 1.7.99.3 (PDB Primary Data), 1.7.2.1 (PDB Primary Data)
UniProt
Find proteins for O68601 (Alcaligenes xylosoxydans xylosoxydans)
Explore O68601 
Go to UniProtKB:  O68601
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO68601
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.226 
  • R-Value Work: 0.201 
  • R-Value Observed: 0.202 
  • Space Group: H 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 91.206α = 90
b = 91.206β = 90
c = 145.866γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-10-28
    Type: Initial release
  • Version 1.1: 2012-05-09
    Changes: Database references, Derived calculations, Non-polymer description, Other, Structure summary, Version format compliance
  • Version 1.2: 2023-12-13
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description