1GCI

THE 0.78 ANGSTROMS STRUCTURE OF A SERINE PROTEASE-BACILLUS LENTUS SUBTILISIN


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 0.78 Å
  • R-Value Free: 0.103 
  • R-Value Observed: 0.099 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The 0.78 A structure of a serine protease: Bacillus lentus subtilisin.

Kuhn, P.Knapp, M.Soltis, S.M.Ganshaw, G.Thoene, M.Bott, R.

(1998) Biochemistry 37: 13446-13452

  • DOI: https://doi.org/10.1021/bi9813983
  • Primary Citation of Related Structures:  
    1GCI

  • PubMed Abstract: 

    Ultrahigh-resolution X-ray diffraction data from cryo-cooled, B. lentus subtilisin crystals has been collected to a resolution of 0.78 A. The refined model coordinates have a rms deviation of 0.22 A relative to the same structure determined at room temperature and 2.0 A resolution. Several regions of main-chain and side-chain disorder have been identified for 21 out of 269 residues in one polypeptide chain. Hydrogen atoms appear as significant peaks in the Fo - Fc difference electron density map, and carbon, nitrogen, and oxygen atoms can be differentiated. The estimated standard deviation (ESD) for all main-chain non-hydrogen bond lengths is 0.009 A and 0.5 degrees for bond angles based on an unrestrained full-matrix least-squares refinement. Hydrogen bonds are resolved in the serine protease catalytic triad (Ser-His-Asp). Electron density is observed for an unusual, short hydrogen bond between aspartic acid and histidine in the catalytic triad. The hydrogen atom, identified by NMR in numerous serine proteases, appears to be shared by the heteroatoms in the bond. This represents the first reported correlation between detailed chemical features identified by NMR and those in a cryo-cooled crystallographic structure determination at ultrahigh resolution. The short hydrogen bond, designated "catalytic hydrogen bond", occurs as part of an elaborate hydrogen bond network, involving Asp of the catalytic triad. While unusual, these features appear to have conserved analogues in other serine protease families although specific details differ from family to family.


  • Organizational Affiliation

    Stanford Synchrotron Radiation Laboratory, Stanford University, California 94309, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SUBTILISIN269Lederbergia lentaMutation(s): 0 
EC: 3.4.21.62
UniProt
Find proteins for P29600 (Lederbergia lenta)
Explore P29600 
Go to UniProtKB:  P29600
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP29600
Sequence Annotations
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  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 0.78 Å
  • R-Value Free: 0.103 
  • R-Value Observed: 0.099 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 52.65α = 90
b = 61.25β = 90
c = 74.75γ = 90
Software Package:
Software NamePurpose
SHELXLrefinement
PROLSQrefinement
MOSFLMdata reduction
CCP4data scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-10-21
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Non-polymer description, Version format compliance
  • Version 1.3: 2023-08-09
    Changes: Database references, Derived calculations, Refinement description