6FID

Bovine trypsin solved by S-SAD on ID30B


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.2 Å
  • R-Value Free: 0.220 
  • R-Value Work: 0.174 

wwPDB Validation 3D Report Full Report


This is version 1.2 of the entry. See complete history

Literature

ID30B - a versatile beamline for macromolecular crystallography experiments at the ESRF.

McCarthy, A.A.Barrett, R.Beteva, A.Caserotto, H.Dobias, F.Felisaz, F.Giraud, T.Guijarro, M.Janocha, R.Khadrouche, A.Lentini, M.Leonard, G.A.Lopez Marrero, M.Malbet-Monaco, S.McSweeney, S.Nurizzo, D.Papp, G.Rossi, C.Sinoir, J.Sorez, C.Surr, J.Svensson, O.Zander, U.Cipriani, F.Theveneau, P.Mueller-Dieckmann, C.

(2018) J Synchrotron Radiat 25: 1249-1260


Macromolecules

Find similar proteins by: Sequence  |  Structure

Entity ID: 1
MoleculeChainsSequence LengthOrganismDetails
Cationic trypsin
A
223Bos taurusMutation(s): 0 
EC: 3.4.21.4
Find proteins for P00760 (Bos taurus)
Go to UniProtKB:  P00760
Small Molecules
Ligands 3 Unique
IDChainsName / Formula / InChI Key2D Diagram3D Interactions
SO4
Query on SO4

Download SDF File 
Download CCD File 
A
SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
 Ligand Interaction
CA
Query on CA

Download SDF File 
Download CCD File 
A
CALCIUM ION
Ca
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
 Ligand Interaction
BEN
Query on BEN

Download SDF File 
Download CCD File 
A
BENZAMIDINE
C7 H8 N2
PXXJHWLDUBFPOL-UHFFFAOYSA-N
 Ligand Interaction
Experimental Data & Validation

Experimental Data

Unit Cell:
Length (Å)Angle (°)
a = 59.947α = 90.00
b = 64.107β = 90.00
c = 69.694γ = 90.00
Software Package:
Software NamePurpose
REFMACrefinement
CRANK2phasing
XDSdata reduction
Aimlessdata scaling

Structure Validation

View Full Validation Report or Ramachandran Plots



Entry History 

Deposition Data

Revision History 

  • Version 1.0: 2018-02-07
    Type: Initial release
  • Version 1.1: 2018-07-18
    Type: Data collection, Database references
  • Version 1.2: 2018-08-08
    Type: Data collection, Database references