1FCQ

CRYSTAL STRUCTURE (MONOCLINIC) OF BEE VENOM HYALURONIDASE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.185 
  • R-Value Observed: 0.192 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal structure of hyaluronidase, a major allergen of bee venom.

Markovic-Housley, Z.Miglierini, G.Soldatova, L.Rizkallah, P.J.Muller, U.Schirmer, T.

(2000) Structure 8: 1025-1035

  • DOI: https://doi.org/10.1016/s0969-2126(00)00511-6
  • Primary Citation of Related Structures:  
    1FCQ, 1FCU, 1FCV

  • PubMed Abstract: 

    Hyaluronic acid (HA) is the most abundant glycosaminoglycan of vertebrate extracellular spaces and is specifically degraded by a beta-1,4 glycosidase. Bee venom hyaluronidase (Hya) shares 30% sequence identity with human hyaluronidases, which are involved in fertilization and the turnover of HA. On the basis of sequence similarity, mammalian enzymes and Hya are assigned to glycosidase family 56 for which no structure has been reported yet.


  • Organizational Affiliation

    Division of Structural Biology Biozentrum University of Basel CH-4056, Basel, Switzerland. zora.housley@unibas.ch


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
HYALURONOGLUCOSAMINIDASE350Apis melliferaMutation(s): 0 
EC: 3.2.1.35
Membrane Entity: Yes 
UniProt
Find proteins for Q08169 (Apis mellifera)
Explore Q08169 
Go to UniProtKB:  Q08169
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ08169
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.185 
  • R-Value Observed: 0.192 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 39.886α = 90
b = 90.229β = 92.36
c = 49.06γ = 90
Software Package:
Software NamePurpose
MOSFLMdata reduction
SCALAdata scaling
SHARPphasing
REFMACrefinement
CCP4data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-10-01
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance