2UY3

ScCTS1_8-chlorotheophylline crystal structure


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.259 
  • R-Value Work: 0.198 
  • R-Value Observed: 0.199 

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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Structure of Saccharomyces Cerevisiae Chitinase 1 and Screening-Based Discovery of Potent Inhibitors.

Hurtado-Guerrero, R.Van Aalten, D.M.F.

(2007) Chem Biol 14: 589

  • DOI: https://doi.org/10.1016/j.chembiol.2007.03.015
  • Primary Citation of Related Structures:  
    2UY2, 2UY3, 2UY4, 2UY5

  • PubMed Abstract: 

    Chitinases hydrolyse the beta(1,4)-glycosidic bonds of chitin, an essential fungal cell wall component. Genetic data on a subclass of fungal family 18 chitinases have suggested a role in cell wall morphology. Specific inhibitors of these enzymes would be useful as tools to study their role in cell wall morphogenesis and could possess antifungal properties. Here, we describe the crystallographic structure of a fungal "plant-type" family 18 chitinase, that of Saccharomyces cerevisiae CTS1. The enzyme is active against 4-methylumbelliferyl chitooligosaccharides and displays an unusually low pH optimum for activity. A library screen against ScCTS1 yielded hits with Ki 's as low as 3.2 microM. Crystal structures of ScCTS1 in complex with inhibitors from three series reveal striking mimicry of carbohydrate substrate by small aromatic moieties and a pocket that could be further exploited in optimization of these inhibitors.


  • Organizational Affiliation

    Division of Biological Chemistry & Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ENDOCHITINASE294Saccharomyces cerevisiaeMutation(s): 0 
EC: 3.2.1.14
UniProt
Find proteins for P29029 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P29029 
Go to UniProtKB:  P29029
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP29029
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
H33
Query on H33

Download Ideal Coordinates CCD File 
B [auth A]8-CHLORO-1,3-DIMETHYL-3,7-DIHYDRO-1H-PURINE-2,6-DIONE
C7 H7 Cl N4 O2
RYIGNEOBDRVTHA-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
H33 Binding MOAD:  2UY3 Ki: 6.00e+5 (nM) from 1 assay(s)
PDBBind:  2UY3 Ki: 6.00e+5 (nM) from 1 assay(s)
BindingDB:  2UY3 Ki: 3.40e+5 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.259 
  • R-Value Work: 0.198 
  • R-Value Observed: 0.199 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 73.411α = 90
b = 112.709β = 90
c = 37.331γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
SCALEPACKdata scaling
MOLREPphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-04-24
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.2: 2023-12-13
    Changes: Data collection, Database references, Other, Refinement description