1VR3 | pdb_00001vr3

Crystal structure of Acireductone dioxygenase (13543033) from Mus musculus at 2.06 A resolution

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.06 Å
  • R-Value Free: 
    0.195 (Depositor), 0.210 (DCC) 
  • R-Value Work: 
    0.162 (Depositor), 0.170 (DCC) 
  • R-Value Observed: 
    0.164 (Depositor) 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history. 


Literature

Crystal structure of acireductone dioxygenase (ARD) from Mus musculus at 2.06 angstrom resolution.

Xu, Q., Schwarzenbacher, R., Krishna, S.S., McMullan, D., Agarwalla, S., Quijano, K., Abdubek, P., Ambing, E., Axelrod, H., Biorac, T., Canaves, J.M., Chiu, H.J., Elsliger, M.A., Grittini, C., Grzechnik, S.K., DiDonato, M., Hale, J., Hampton, E., Han, G.W., Haugen, J., Hornsby, M., Jaroszewski, L., Klock, H.E., Knuth, M.W., Koesema, E., Kreusch, A., Kuhn, P., Miller, M.D., Moy, K., Nigoghossian, E., Paulsen, J., Reyes, R., Rife, C., Spraggon, G., Stevens, R.C., van den Bedem, H., Velasquez, J., White, A., Wolf, G., Hodgson, K.O., Wooley, J., Deacon, A.M., Godzik, A., Lesley, S.A., Wilson, I.A.

(2006) Proteins 64: 808-813


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Acireductone dioxygenase191Mus musculusMutation(s): 9 
EC: 1.13.11 (PDB Primary Data), 1.13.11.54 (UniProt), 1.13.11.53 (UniProt)
UniProt
Find proteins for Q99JT9 (Mus musculus)
Explore Q99JT9 
Go to UniProtKB:  Q99JT9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ99JT9
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.06 Å
  • R-Value Free:  0.195 (Depositor), 0.210 (DCC) 
  • R-Value Work:  0.162 (Depositor), 0.170 (DCC) 
  • R-Value Observed: 0.164 (Depositor) 
Space Group: P 41 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 79.136α = 90
b = 79.136β = 90
c = 114.128γ = 90
Software Package:
Software NamePurpose
XDSdata scaling
SCALAdata scaling
autoSHARPphasing
REFMACrefinement
XDSdata reduction
CCP4data scaling

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-02-15
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.3: 2023-01-25
    Changes: Database references, Derived calculations
  • Version 1.4: 2024-11-20
    Changes: Data collection, Structure summary