4P2P

AN INDEPENDENT CRYSTALLOGRAPHIC REFINEMENT OF PORCINE PHOSPHOLIPASE A2 AT 2.4 ANGSTROMS RESOLUTION

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Observed: 0.210 

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This is version 1.3 of the entry. See complete history. 


Literature

An independent crystallographic refinement of porcine phospholipase A2 at 2.4 A resolution

Finzel, B.C., Ohlendorf, D.H., Weber, P.C., Salemme, F.R.

(1991) Acta Crystallogr B 47: 558-559

  • DOI: https://doi.org/10.1107/s0108768190012939
  • Primary Citation of Related Structures:  
    4P2P

  • PubMed Abstract: 

    Porcine phospholipase A2 (Mr = 13,980), trigonal, P3(1)21, a = b = 69.4, c = 70.4 A, one molecule per asymmetric unit, lambda (Cu K alpha) = 1.54 A. Model incorporating 975 protein atoms and eight solvent molecules refined by restrained least-squares fit to a residual R = 0.21 for 6382 reflections from 5 to 2.4 A resolution.

    • Organizational Affiliation: 

    E. I. du Pont de Nemours and Company, Central Research and Development Department, Wilmington, DE 19880-0228.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PHOSPHOLIPASE A2124Sus scrofaMutation(s): 0 
EC: 3.1.1.4
Membrane Entity: Yes 
UniProt
Find proteins for P00592 (Sus scrofa)
Explore P00592 
Go to UniProtKB:  P00592
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00592
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Observed: 0.210 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 69.4α = 90
b = 69.4β = 90
c = 70.4γ = 120
Software Package:
Software NamePurpose
PROLSQrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1992-01-15
    Type: Initial release
  • Version 1.1: 2008-03-03
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2017-11-29
    Changes: Derived calculations, Other