2F0Z

Crystal Structure of the Human Sialidase Neu2 in Complex with Zanamivir inhibitor


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.280 
  • R-Value Work: 0.192 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history


Literature

Crystal Structure of the Human Sialidase Neu2 in Complex with Zanamivir inhibitor

Chavas, L.M.G.Kato, R.McKimm-Breschkin, J.Colman, P.M.Fusi, P.Tringali, C.Venerando, B.Tettamanti, G.Monti, E.Wakatsuki, S.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Sialidase 2382Homo sapiensMutation(s): 0 
EC: 3.2.1.18
UniProt & NIH Common Fund Data Resources
Find proteins for Q9Y3R4 (Homo sapiens)
Explore Q9Y3R4 
Go to UniProtKB:  Q9Y3R4
PHAROS:  Q9Y3R4
GTEx:  ENSG00000115488 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9Y3R4
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ZMR
Query on ZMR

Download Ideal Coordinates CCD File 
B [auth A]ZANAMIVIR
C12 H20 N4 O7
ARAIBEBZBOPLMB-UFGQHTETSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
ZMR BindingDB:  2F0Z Ki: min: 5700, max: 1.70e+4 (nM) from 2 assay(s)
IC50: min: 7800, max: 1.64e+4 (nM) from 4 assay(s)
PDBBind:  2F0Z Ki: 1.70e+4 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.280 
  • R-Value Work: 0.192 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 85.51α = 90
b = 85.68β = 90
c = 92.09γ = 90
Software Package:
Software NamePurpose
CNSrefinement
PDB_EXTRACTdata extraction
HKL-2000data reduction
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: 2006-11-21
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Data collection, Database references, Derived calculations
  • Version 1.4: 2023-10-25
    Changes: Data collection, Database references, Refinement description, Structure summary