2PKA | pdb_00002pka

REFINED 2 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF PORCINE PANCREATIC KALLIKREIN A, A SPECIFIC TRYPSIN-LIKE SERINE PROTEINASE. CRYSTALLIZATION, STRUCTURE DETERMINATION, CRYSTALLOGRAPHIC REFINEMENT, STRUCTURE AND ITS COMPARISON WITH BOVINE TRYPSIN

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.05 Å
  • R-Value Work: 
    0.220 (Depositor) 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history. 


Literature

Refined 2 A X-ray crystal structure of porcine pancreatic kallikrein A, a specific trypsin-like serine proteinase. Crystallization, structure determination, crystallographic refinement, structure and its comparison with bovine trypsin.

Bode, W., Chen, Z., Bartels, K., Kutzbach, C., Schmidt-Kastner, G., Bartunik, H.

(1983) J Mol Biology 164: 237-282


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
KALLIKREIN AA,
C [auth X]		80Sus scrofaMutation(s): 0 
EC: 3.4.21.35
UniProt
Find proteins for P00752 (Sus scrofa)
Explore P00752 
Go to UniProtKB:  P00752
Entity Groups  
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UniProt GroupP00752
Sequence Annotations
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  • Reference Sequence
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(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
KALLIKREIN AB,
D [auth Y]		152Sus scrofaMutation(s): 0 
EC: 3.4.21.35
UniProt
Find proteins for P00752 (Sus scrofa)
Explore P00752 
Go to UniProtKB:  P00752
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00752
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.05 Å
  • R-Value Work:  0.220 (Depositor) 
Space Group: P 41 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 90.2α = 90
b = 90.2β = 90
c = 159.4γ = 90
Software Package:
Software NamePurpose
EREFrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1984-07-19
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-06-05
    Changes: Data collection, Database references, Derived calculations, Other
  • Version 1.4: 2024-10-23
    Changes: Structure summary