2F91

1.2A resolution structure of a crayfish trypsin complexed with a peptide inhibitor, SGTI

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.20 Å
  • R-Value Free: 0.182 

wwPDB Validation   3D Report Full Report


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


Literature

Enzyme:Substrate Hydrogen Bond Shortening during the Acylation Phase of Serine Protease Catalysis.

Fodor, K., Harmat, V., Neutze, R., Szilagyi, L., Graf, L., Katona, G.

(2006) Biochemistry 45: 2114-2121

  • DOI: https://doi.org/10.1021/bi0517133
  • Primary Citation of Related Structures:  
    2F91

  • PubMed Abstract: 

    Atomic resolution (

    • Organizational Affiliation: 

    Biotechnology Research Group of the Hungarian Academy of Sciences, Pázmány Street 1/C, 1117 Budapest, Hungary.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
hepatopancreas trypsin237Astacus leptodactylusMutation(s): 1 
EC: 3.4.21.4
UniProt
Find proteins for Q52V24 (Astacus leptodactylus)
Explore Q52V24 
Go to UniProtKB:  Q52V24
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ52V24
Sequence Annotations
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  • Reference Sequence
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Serine protease inhibitor I/II35N/AMutation(s): 0 
UniProt
Find proteins for O46162 (Schistocerca gregaria)
Explore O46162 
Go to UniProtKB:  O46162
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO46162
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.20 Å
  • R-Value Free: 0.182 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 41.283α = 90
b = 59.673β = 90
c = 97.302γ = 90
Software Package:
Software NamePurpose
MOSFLMdata reduction
SCALAdata scaling
MOLREPphasing
SHELXL-97refinement
CCP4data scaling

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-04-18
    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: 2023-08-30
    Changes: Data collection, Database references, Derived calculations, Refinement description