4KWS

Crystal structure of d-mannonate dehydratase from chromohalobacter salexigens complexed with Mg and glycerol


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.64 Å
  • R-Value Free: 0.163 
  • R-Value Work: 0.139 
  • R-Value Observed: 0.140 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Crystal structure of d-mannonate dehydratase from chromohalobacter salexigens complexed with Mg and glycerol

Fedorov, A.A.Fedorov, E.V.Wichelecki, D.Gerlt, J.A.Almo, S.C.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
D-mannonate dehydratase
A, B, C, D, E
A, B, C, D, E, F, G, H
405Chromohalobacter salexigens DSM 3043Mutation(s): 0 
Gene Names: Csal_2974
EC: 4.2.1.8
UniProt
Find proteins for Q1QT89 (Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11))
Explore Q1QT89 
Go to UniProtKB:  Q1QT89
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ1QT89
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
GOL
Query on GOL

Download Ideal Coordinates CCD File 
BA [auth F]
EA [auth G]
GA [auth H]
J [auth A]
N [auth B]
BA [auth F],
EA [auth G],
GA [auth H],
J [auth A],
N [auth B],
Q [auth C],
U [auth D],
Y [auth E]
GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
CL
Query on CL

Download Ideal Coordinates CCD File 
CA [auth F],
K [auth A],
R [auth C],
Z [auth E]
CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
MG
Query on MG

Download Ideal Coordinates CCD File 
AA [auth F]
DA [auth G]
FA [auth H]
I [auth A]
L [auth A]
AA [auth F],
DA [auth G],
FA [auth H],
I [auth A],
L [auth A],
M [auth B],
O [auth B],
P [auth C],
S [auth C],
T [auth D],
V [auth D],
W [auth D],
X [auth E]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.64 Å
  • R-Value Free: 0.163 
  • R-Value Work: 0.139 
  • R-Value Observed: 0.140 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 195.273α = 90
b = 85.762β = 110.31
c = 195.097γ = 90
Software Package:
Software NamePurpose
CBASSdata collection
BALBESphasing
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-05-28
    Type: Initial release
  • Version 1.1: 2023-09-20
    Changes: Data collection, Database references, Derived calculations, Refinement description