4X0N

Porcine pancreatic alpha-amylase in complex with helianthamide, a novel proteinaceous inhibitor

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.226 
  • R-Value Work: 0.182 
  • R-Value Observed: 0.184 

wwPDB Validation   3D Report Full Report


This is version 2.1 of the entry. See complete history. 


Literature

Structural Templating and Guided Refolding of the Potent Naturally Occurring Peptide Helianthamide Within the Active Site of Amylase, a Diabetes and Obesity Therapeutic Target

Tysoe, C., Williams, L.K., Keyzers, R., Nguyen, N.T., Aguda, A., Zhang, X., Tarling, C.A., Andersen, R.J., Brayer, G.D., Withers, S.G.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Pancreatic alpha-amylase496Sus scrofaMutation(s): 0 
EC: 3.2.1.1
UniProt
Find proteins for P00690 (Sus scrofa)
Explore P00690 
Go to UniProtKB:  P00690
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00690
Sequence Annotations
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  • Reference Sequence
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Helianthamide44Stichodactyla helianthusMutation(s): 0 
UniProt
Find proteins for A0A0X1KGZ5 (Stichodactyla helianthus)
Explore A0A0X1KGZ5 
Go to UniProtKB:  A0A0X1KGZ5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0X1KGZ5
Sequence Annotations
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  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
PCA
Query on PCA
A
L-PEPTIDE LINKINGC5 H7 N O3GLN
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.226 
  • R-Value Work: 0.182 
  • R-Value Observed: 0.184 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 43.75α = 90
b = 103.28β = 90
c = 111.896γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
CNSphasing

Structure Validation

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View more in-depth experimental data
Entry History & Funding Information

Deposition Data

Funding OrganizationLocationGrant Number
Canadian Institutes of Health Research (CIHR)Canada--

Revision History  (Full details and data files)

  • Version 1.0: 2015-11-25
    Type: Initial release
  • Version 1.1: 2017-09-27
    Changes: Author supporting evidence, Derived calculations
  • Version 2.0: 2020-01-08
    Changes: Author supporting evidence, Polymer sequence
  • Version 2.1: 2023-09-27
    Changes: Data collection, Database references, Derived calculations, Refinement description