1GOI

Crystal structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 A resolution

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.45 Å
  • R-Value Free: 0.220 
  • R-Value Observed: 0.160 

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This is version 1.2 of the entry. See complete history. 


Literature

Structure of the D140N Mutant of Chitinase B from Serratia Marcescens at 1.45 A Resolution.

Kolstad, G., Synstad, B., Eijsink, V.G.H., Van Aalten, D.M.F.

(2002) Acta Crystallogr D Biol Crystallogr 58: 377

  • DOI: https://doi.org/10.1107/s0907444901018972
  • Primary Citation of Related Structures:  
    1GOI

  • PubMed Abstract: 

    The crystal structure of the inactive D140N mutant of Serratia marcescens was refined to 1.45 A resolution. The structure of the mutant was essentially identical to that of the wild type, with the exception of a rotation of Asp142 in the catalytic centre. In the mutant, this residue interacts with the catalytic acid (Glu144) and not with residue 140 as in the wild type. Thus, the 500-fold decrease in activity in the D140N mutant seems to be largely mediated by an effect on Asp142, confirming the crucial role of the latter residue in catalysis.

    • Organizational Affiliation: 

    Department of Chemistry and Biotechnology, Agricultural University of Norway, 1432 As, Norway.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CHITINASE B
A, B
499Serratia marcescensMutation(s): 1 
EC: 3.2.1.14
UniProt
Find proteins for P11797 (Serratia marcescens)
Explore P11797 
Go to UniProtKB:  P11797
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP11797
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
SO4
Query on SO4
Download Ideal Coordinates CCD File 
I [auth A],
P [auth B],
Q [auth B],
R [auth B]		SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
GOL
Query on GOL
Download Ideal Coordinates CCD File 
C [auth A]
D [auth A]
E [auth A]
F [auth A]
G [auth A]
C [auth A],
D [auth A],
E [auth A],
F [auth A],
G [auth A],
H [auth A],
J [auth B],
K [auth B],
L [auth B],
M [auth B],
N [auth B],
O [auth B]
GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.45 Å
  • R-Value Free: 0.220 
  • R-Value Observed: 0.160 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 55.904α = 90
b = 104.016β = 90
c = 186.524γ = 90
Software Package:
Software NamePurpose
SHELXL-97refinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-11-15
    Type: Initial release
  • Version 1.1: 2011-09-14
    Changes: Atomic model, Database references, Derived calculations, Non-polymer description, Other, Structure summary, Version format compliance
  • Version 1.2: 2023-12-13
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description