1HYL

THE 1.8 A STRUCTURE OF COLLAGENASE FROM HYPODERMA LINEATUM


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Work: 0.183 
  • R-Value Observed: 0.183 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

1.8 A structure of Hypoderma lineatum collagenase: a member of the serine proteinase family.

Broutin, I.Arnoux, B.Riche, C.Lecroisey, A.Keil, B.Pascard, C.Ducruix, A.

(1996) Acta Crystallogr D Biol Crystallogr 52: 380-392

  • DOI: https://doi.org/10.1107/S090744499501184X
  • Primary Citation of Related Structures:  
    1HYL, 2HLC

  • PubMed Abstract: 

    Collagenase from the fly larvae Hypoderma lineatum cleaves triple-helical collagen in a single region. It was crystallized at neutral pH in the absence of inhibitor and 1.8 A data were collected using synchrotron radiation and a Mark II prototype detector. The structure was solved by combining multiple isomorphous replacement methods and rotation translation function in real space. Refinement between 7 and 1.8 A using the program X-PLOR led to a final R factor of 16.9%. The overall fold is similar to that of other trypsin-like enzymes but the structure differs mainly by the presence of a beta-sheet at position 31-44. The two embedded molecules of the asymmetric unit are related by a pseudo twofold axis. The beta-sheet 31-44 of one molecule is involved in hydrogen bonds with binding-pocket residues of the other molecule. It thus completely prevents access to the active site. The specificity of this enzyme probably results from the position of Phe192 and Tyr99 at the entrance of the active site.


  • Organizational Affiliation

    Institut de Chimie des Substances Naturelles, CNRS 91198 Gif sur Yvette, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
HYPODERMA LINEATUM COLLAGENASE
A, B
230Hypoderma lineatumMutation(s): 0 
EC: 3.4.21
UniProt
Find proteins for P08897 (Hypoderma lineatum)
Explore P08897 
Go to UniProtKB:  P08897
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP08897
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Work: 0.183 
  • R-Value Observed: 0.183 
  • Space Group: I 4 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 111.7α = 90
b = 111.7β = 90
c = 165.8γ = 90
Software Package:
Software NamePurpose
MADNESdata collection
X-PLORmodel building
X-PLORrefinement
MADNESdata reduction
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1995-07-31
    Type: Initial release
  • Version 1.1: 2008-03-03
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance