4Z9N | pdb_00004z9n

ABC transporter / periplasmic binding protein from Brucella ovis with glutathione bound


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free: 
    0.183 (Depositor), 0.180 (DCC) 
  • R-Value Work: 
    0.152 (Depositor), 0.150 (DCC) 
  • R-Value Observed: 
    0.152 (Depositor) 

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 GSHClick on this verticalbar to view details

This is version 1.0 of the entry. See complete history


Literature

ABC transporter / periplasmic binding protein from Brucella ovis with glutathione bound

Seattle Structural Genomics Center for Infectious Disease (SSGCID)

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Amino acid ABC transporter, periplasmic amino acid-binding protein
A, B, C, D, E
328Brucella ovis ATCC 25840Mutation(s): 0 
Gene Names: BOV_0736
UniProt
Find proteins for A0A0M3KL33 (Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512))
Explore A0A0M3KL33 
Go to UniProtKB:  A0A0M3KL33
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0M3KL33
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
GSH
Query on GSH

Download Ideal Coordinates CCD File 
G [auth A]
L [auth B]
Q [auth C]
U [auth D]
W [auth E]
GLUTATHIONE
C10 H17 N3 O6 S
RWSXRVCMGQZWBV-WDSKDSINSA-N
EDO
Query on EDO

Download Ideal Coordinates CCD File 
I [auth A]
J [auth A]
N [auth B]
O [auth B]
S [auth C]
1,2-ETHANEDIOL
C2 H6 O2
LYCAIKOWRPUZTN-UHFFFAOYSA-N
NA
Query on NA

Download Ideal Coordinates CCD File 
H [auth A]
K [auth A]
M [auth B]
P [auth B]
R [auth C]
SODIUM ION
Na
FKNQFGJONOIPTF-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free:  0.183 (Depositor), 0.180 (DCC) 
  • R-Value Work:  0.152 (Depositor), 0.150 (DCC) 
  • R-Value Observed: 0.152 (Depositor) 
Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 93.99α = 90
b = 76.93β = 94.07
c = 131.47γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XSCALEdata scaling
PHENIXphasing

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 GSHClick on this verticalbar to view details

Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-06-17
    Type: Initial release