1TO9

Crystal structure of THI-4 protein from Bacillus subtilis

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.210 
  • R-Value Observed: 0.212 

wwPDB Validation   3D Report Full Report


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


Literature

Crystal structure of THI-4 protein from Bacillus subtilis

Rajan, S.S., Shuvalova, L., Yang, X., Hussar, C., Collart, F., Anderson, W.F.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
THI-4 protein260Bacillus subtilisMutation(s): 6 
Gene Names: TENA, BSU11650
UniProt
Find proteins for P25052 (Bacillus subtilis (strain 168))
Explore P25052 
Go to UniProtKB:  P25052
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP25052
Sequence Annotations
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  • Reference Sequence
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
THI-4 protein260Bacillus subtilisMutation(s): 6 
Gene Names: TENA, BSU11650
UniProt
Find proteins for P25052 (Bacillus subtilis (strain 168))
Explore P25052 
Go to UniProtKB:  P25052
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP25052
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
HMH
Query on HMH
Download Ideal Coordinates CCD File 
C [auth A],
D [auth B]		4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE
C6 H9 N3 O
VUTBELPREDJDDH-UHFFFAOYSA-N
Modified Residues  2 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
CSD
Query on CSD
B
L-PEPTIDE LINKINGC3 H7 N O4 SCYS
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.210 
  • R-Value Observed: 0.212 
  • Space Group: P 41 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 58.38α = 90
b = 58.38β = 90
c = 296.24γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data reduction
SCALEPACKdata scaling
SOLVEphasing

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: 2004-08-10
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.3: 2014-11-19
    Changes: Non-polymer description