1X6N

Crystal structure of S. marcescens chitinase A mutant W167A in complex with allosamidin

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.238 
  • R-Value Work: 0.214 
  • R-Value Observed: 0.214 

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Ligand Structure Quality Assessment 


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


Literature

Muation of Trp167 at the -3 subsite of the chitin-binding cleft of S. marcescens chitinase A causes enhanced transglycosylation

Aronson Jr., N.N., Halloran, B.A., Alexyev, M.F., Zhou, X.E., Wang, Y., Meehan, E.J., Chen, L.

To be published.

Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Chitinase A563Serratia marcescensMutation(s): 1 
Gene Names: chiA
EC: 3.2.1.14
UniProt
Find proteins for P07254 (Serratia marcescens)
Explore P07254 
Go to UniProtKB:  P07254
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP07254
Sequence Annotations
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  • Reference Sequence
Oligosaccharides

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Entity ID: 2
MoleculeChains Length2D Diagram Glycosylation3D Interactions
2-acetamido-2-deoxy-beta-D-allopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-allopyranose
B
2N/A
Glycosylation Resources
GlyTouCan:  G77950XB
GlyCosmos:  G77950XB
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
AMI
Query on AMI
Download Ideal Coordinates CCD File 
C [auth A]ALLOSAMIZOLINE
C9 H16 N2 O4
MKJAYSJDHSEFRI-PVFLNQBWSA-N
Biologically Interesting Molecules (External Reference) 1 Unique
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.238 
  • R-Value Work: 0.214 
  • R-Value Observed: 0.214 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 76.67α = 90
b = 133.07β = 90
c = 192.22γ = 90
Software Package:
Software NamePurpose
CNSrefinement
HKL-2000data reduction
SCALEPACKdata scaling
CNSphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-07-26
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2016-11-09
    Changes: Non-polymer description
  • Version 1.4: 2021-10-20
    Changes: Advisory, Database references, Structure summary
  • Version 2.0: 2022-04-13
    Changes: Atomic model, Data collection, Derived calculations, Non-polymer description, Structure summary
  • Version 2.1: 2023-08-23
    Changes: Data collection, Refinement description