2RDX

Crystal structure of mandelate racemase/muconate lactonizing enzyme from Roseovarius nubinhibens ISM

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.256 
  • R-Value Work: 0.194 
  • R-Value Observed: 0.196 

wwPDB Validation   3D Report Full Report


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


Literature

Crystal structure of mandelate racemase/muconate lactonizing enzyme from Roseovarius nubinhibens ISM.

Patskovsky, Y., Bonanno, J.B., Sauder, J.M., Gilmore, M., Ozyurt, S., Lau, C., Maletic, M., Gheyi, T., Wasserman, S.R., Koss, J., Gerlt, J.A., 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
Mandelate racemase/muconate lactonizing enzyme, putative
A, B, C, D, E
A, B, C, D, E, F, G, H
379Roseovarius nubinhibens ISMMutation(s): 0 
Gene Names: ISM_14070
UniProt
Find proteins for A3SNF8 (Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM))
Explore A3SNF8 
Go to UniProtKB:  A3SNF8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA3SNF8
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
GOL
Query on GOL
Download Ideal Coordinates CCD File 
J [auth A]
K [auth A]
N [auth C]
P [auth D]
S [auth F]
J [auth A],
K [auth A],
N [auth C],
P [auth D],
S [auth F],
U [auth G],
W [auth H]
GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
MG
Query on MG
Download Ideal Coordinates CCD File 
I [auth A]
L [auth B]
M [auth C]
O [auth D]
Q [auth E]
I [auth A],
L [auth B],
M [auth C],
O [auth D],
Q [auth E],
R [auth F],
T [auth G],
V [auth H]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.256 
  • R-Value Work: 0.194 
  • R-Value Observed: 0.196 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 169.415α = 90
b = 169.219β = 90
c = 223.476γ = 90
Software Package:
Software NamePurpose
SHELXmodel building
REFMACrefinement
MAR345data collection
HKL-2000data reduction
HKL-2000data scaling
SHELXphasing

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: 2007-10-09
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Source and taxonomy, Version format compliance
  • Version 1.2: 2017-10-25
    Changes: Refinement description
  • Version 1.3: 2018-11-14
    Changes: Data collection, Structure summary
  • Version 1.4: 2021-02-03
    Changes: Database references, Derived calculations, Structure summary
  • Version 1.5: 2024-02-21
    Changes: Data collection, Database references