7DIB

Crystal structure of D-threonine aldolase from Filomicrobium marinum


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.254 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.213 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Cbeta-Selective Aldol Addition of d-Threonine Aldolase by Spatial Constraint of Aldehyde Binding.

Park, S.-H.Seo, H.Seok, J.Kim, H.Kwon, K.K.Yeom, S.-J.Lee, S.-G.Kim, K.-J.

(2021) ACS Catal 11: 6892-6899


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
D-threonine aldolase
A, B
396Candidatus Filomicrobium marinumMutation(s): 0 
Gene Names: YBN1229_v1_3680
EC: 4.1.2.42
UniProt
Find proteins for A0A0D6JKM4 (Candidatus Filomicrobium marinum)
Explore A0A0D6JKM4 
Go to UniProtKB:  A0A0D6JKM4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0D6JKM4
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
LLP
Query on LLP
A, B
L-PEPTIDE LINKINGC14 H22 N3 O7 PLYS
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.254 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.213 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 70.965α = 90
b = 178.051β = 90
c = 65.458γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling
MOLREPphasing
PDB_EXTRACTdata extraction

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2021-08-04
    Type: Initial release
  • Version 1.1: 2023-11-29
    Changes: Data collection, Database references, Refinement description