6BZC

Crystal Structure of Glucose-6-phosphate Isomerase from Elizabethkingia anophelis with bound Glucose-6-phosphate


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.05 Å
  • R-Value Free: 0.276 
  • R-Value Work: 0.207 
  • R-Value Observed: 0.209 

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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Crystal Structure of Glucose-6-phosphate Isomerase from Elizabethkingia anophelis with bound Glucose-6-phosphate

Dranow, D.M.Mayclin, S.J.Lorimer, D.D.Edwards, T.E.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Glucose-6-phosphate isomerase
A, B
555Elizabethkingia anophelis NUHP1Mutation(s): 0 
Gene Names: pgiBD94_3890
EC: 5.3.1.9
UniProt
Find proteins for A0A077EQ93 (Elizabethkingia anophelis NUHP1)
Explore A0A077EQ93 
Go to UniProtKB:  A0A077EQ93
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A077EQ93
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 69.28α = 90
b = 102.14β = 90
c = 153.73γ = 90
Software Package:
Software NamePurpose
XDSdata reduction
XSCALEdata scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACTdata extraction

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-01-10
    Type: Initial release
  • Version 1.1: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Data collection, Derived calculations, Structure summary
  • Version 1.2: 2023-10-04
    Changes: Data collection, Database references, Refinement description, Structure summary