3EWB

Crystal structure of N-terminal domain of putative 2-isopropylmalate synthase from Listeria monocytogenes


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.245 
  • R-Value Work: 0.194 
  • R-Value Observed: 0.196 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Crystal structure of N-terminal domain of putative 2-isopropylmalate synthase from Listeria monocytogenes.

Ramagopal, U.A.Toro, R.Gilmore, M.Hu, S.Maletic, M.Rodgers, L.Burley, S.K.Almo, S.C.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
2-isopropylmalate synthaseA [auth X]293Listeria monocytogenes serotype 4b str. F2365Mutation(s): 0 
Gene Names: leuALMOf2365_2010
EC: 2.3.3.13
UniProt
Find proteins for Q71Y35 (Listeria monocytogenes serotype 4b (strain F2365))
Explore Q71Y35 
Go to UniProtKB:  Q71Y35
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ71Y35
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A [auth X]L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.245 
  • R-Value Work: 0.194 
  • R-Value Observed: 0.196 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 72.063α = 90
b = 72.063β = 90
c = 106.622γ = 120
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
REFMACrefinement
PDB_EXTRACTdata extraction
CBASSdata collection
HKL-2000data reduction
PHENIXphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2008-12-23
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2017-10-25
    Changes: Refinement description
  • Version 1.3: 2021-02-10
    Changes: Database references, Derived calculations, Structure summary
  • Version 1.4: 2023-12-27
    Changes: Data collection, Database references