5AQE

Cooperative bio-metallic selectivity in a tailored protease enables creation of a C-C cross-coupling Heckase


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.10 Å
  • R-Value Free: 0.088 
  • R-Value Work: 0.076 
  • R-Value Observed: 0.077 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

Bisubstrate Localisation by a Tailored Serine Protease Allows Creation of a Heck-Ase

Sharma, M.Diaz-Rodriguez, A.Offen, W.A.Pordea, A.Wormald, M.R.Mcdonough, M.Davies, G.J.Davis, B.G.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SUBTILISIN SAVINASE269Lederbergia lentaMutation(s): 0 
EC: 3.4.21.62
UniProt
Find proteins for P29600 (Lederbergia lenta)
Explore P29600 
Go to UniProtKB:  P29600
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP29600
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 5 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
VOD
Query on VOD

Download Ideal Coordinates CCD File 
B [auth A](4-VINYLPHENYL)METHANESULFONIC ACID
C9 H10 O3 S
SDXKWPVFZWZYNK-UHFFFAOYSA-N
SO4
Query on SO4

Download Ideal Coordinates CCD File 
C [auth A]SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
GOL
Query on GOL

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E [auth A],
F [auth A]
GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
CA
Query on CA

Download Ideal Coordinates CCD File 
D [auth A]CALCIUM ION
Ca
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
CL
Query on CL

Download Ideal Coordinates CCD File 
G [auth A]CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.10 Å
  • R-Value Free: 0.088 
  • R-Value Work: 0.076 
  • R-Value Observed: 0.077 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 52.648α = 90
b = 61.246β = 90
c = 74.615γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
Aimlessdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-10-07
    Type: Initial release
  • Version 1.1: 2024-01-10
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description