5M0T | pdb_00005m0t

Alpha-ketoglutarate-dependent non-heme iron oxygenase EasH

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 
    0.244 (Depositor), 0.250 (DCC) 
  • R-Value Work: 
    0.218 (Depositor), 0.230 (DCC) 
  • R-Value Observed: 
    0.219 (Depositor) 

Starting Model: experimental
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This is version 1.2 of the entry. See complete history. 


Literature

Structural characterization of EasH (Aspergillus japonicus) - an oxidase involved in cycloclavine biosynthesis.

Jakubczyk, D., Caputi, L., Stevenson, C.E., Lawson, D.M., O'Connor, S.E.

(2016) Chem Commun (Camb) 52: 14306-14309

  • DOI: https://doi.org/10.1039/c6cc08438a
  • Primary Citation of Related Structures:  
    5M0T

  • PubMed Abstract: 

    Aj_EasH is a non-heme iron- and α-keto-glutarate-dependent oxidase that is responsible for an unusual cyclopropyl ring formation in the biosynthesis of the fungal ergot alkaloid cycloclavine. The three dimensional structure of Aj_EasH (2.2 Å resolution) reported here provides insight into the mechanism of this unusual and complex reaction.

    • Organizational Affiliation: 

    Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK. Sarah.oconnor@jic.ac.uk.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Alpha-ketoglutarate-dependent non-heme iron oxygenase EasH
A, B
294Aspergillus japonicusMutation(s): 0 
UniProt
Find proteins for A0A1L1QK38 (Aspergillus japonicus)
Explore A0A1L1QK38 
Go to UniProtKB:  A0A1L1QK38
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A1L1QK38
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
AKG
Query on AKG
Download Ideal Coordinates CCD File 
D [auth A],
H [auth A],
J [auth B]		2-OXOGLUTARIC ACID
C5 H6 O5
KPGXRSRHYNQIFN-UHFFFAOYSA-N
ZN
Query on ZN
Download Ideal Coordinates CCD File 
E [auth A],
F [auth A],
G [auth A],
K [auth B]		ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
FE2
Query on FE2
Download Ideal Coordinates CCD File 
C [auth A],
I [auth B]		FE (II) ION
Fe
CWYNVVGOOAEACU-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free:  0.244 (Depositor), 0.250 (DCC) 
  • R-Value Work:  0.218 (Depositor), 0.230 (DCC) 
  • R-Value Observed: 0.219 (Depositor) 
Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 40.25α = 90
b = 100.17β = 90
c = 148.88γ = 90
Software Package:
Software NamePurpose
Aimlessdata scaling
REFMACrefinement
PDB_EXTRACTdata extraction
PHASERphasing
XDSdata reduction

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-12-07
    Type: Initial release
  • Version 1.1: 2016-12-14
    Changes: Database references
  • Version 1.2: 2024-01-17
    Changes: Data collection, Database references, Derived calculations, Refinement description