3LUS | pdb_00003lus

Crystal structure of a putative organic hydroperoxide resistance protein with molecule of captopril bound in one of the active sites from Vibrio cholerae O1 biovar eltor str. N16961

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.96 Å
  • R-Value Free: 
    0.227 (Depositor), 0.250 (DCC) 
  • R-Value Work: 
    0.171 (Depositor), 0.190 (DCC) 
  • R-Value Observed: 
    0.173 (Depositor) 

Starting Model: experimental
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wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted X8ZClick on this verticalbar to view details

This is version 1.5 of the entry. See complete history. 


Literature

Crystal structure of a putative organic hydroperoxide resistance protein with molecule of captopril bound in one of the active sites from Vibrio cholerae O1 biovar eltor str. N16961

Nocek, B., Maltseva, N., Makowska-Grzyska, N., Kwon, K., Anderson, W., Joachimiak, A., NIAID

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Organic hydroperoxide resistance protein
A, B
148Vibrio cholerae O1 biovar El Tor str. N16961Mutation(s): 0 
Gene Names: VC_A1006
UniProt
Find proteins for Q9KKU4 (Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961))
Explore Q9KKU4 
Go to UniProtKB:  Q9KKU4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9KKU4
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
X8Z
Query on X8Z
Download Ideal Coordinates CCD File 
C [auth B]L-CAPTOPRIL
C9 H15 N O3 S
FAKRSMQSSFJEIM-RQJHMYQMSA-N
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.96 Å
  • R-Value Free:  0.227 (Depositor), 0.250 (DCC) 
  • R-Value Work:  0.171 (Depositor), 0.190 (DCC) 
  • R-Value Observed: 0.173 (Depositor) 
Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 38.203α = 90
b = 76.198β = 90
c = 79.396γ = 90
Software Package:
Software NamePurpose
SBC-Collectdata collection
MOLREPphasing
Cootmodel building
REFMACrefinement
HKL-3000data reduction
HKL-3000data scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted X8ZClick on this verticalbar to view details

View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-04-21
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.2: 2013-05-01
    Changes: Non-polymer description
  • Version 1.3: 2023-09-06
    Changes: Data collection, Database references, Derived calculations, Refinement description
  • Version 1.4: 2023-11-22
    Changes: Data collection
  • Version 1.5: 2024-10-16
    Changes: Structure summary