4MSO

X-ray crystal structure of a serine hydroxymethyl transferase in apo form from Burkholderia cenocepacia


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.182 
  • R-Value Work: 0.146 
  • R-Value Observed: 0.148 

Starting Model: experimental
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wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

X-ray crystal structure of a serine hydroxymethyl transferase in apo form from Burkholderia cenocepacia

Fairman, J.W.Jensen, M.M.Sullivan, A.H.Abendroth, J.Edwards, T.E.Lorimer, D.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Serine hydroxymethyltransferase
A, B
423Burkholderia cenocepacia J2315Mutation(s): 0 
Gene Names: glyAglyA1BceJ2315_31420BCAL3197
EC: 2.1.2.1
UniProt
Find proteins for B4ECY9 (Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610))
Explore B4ECY9 
Go to UniProtKB:  B4ECY9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupB4ECY9
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 55.28α = 90
b = 72.58β = 90
c = 182.12γ = 90
Software Package:
Software NamePurpose
XSCALEdata scaling
PHASERphasing
REFMACrefinement
PDB_EXTRACTdata extraction

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-12-11
    Type: Initial release
  • Version 1.1: 2023-09-20
    Changes: Data collection, Database references, Derived calculations, Refinement description