3DPJ

The crystal structure of a TetR transcription regulator from Silicibacter pomeroyi DSS


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.243 
  • R-Value Work: 0.193 
  • R-Value Observed: 0.196 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

The crystal structure of a TetR transcription regulator from Silicibacter pomeroyi DSS

Tan, K.Li, H.Freeman, L.Joachimiak, A.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Transcription regulator, TetR family
A, B, C, D, E
A, B, C, D, E, F, G, H
194Ruegeria pomeroyiMutation(s): 0 
Gene Names: SPO1902
UniProt
Find proteins for Q5LS67 (Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3))
Explore Q5LS67 
Go to UniProtKB:  Q5LS67
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5LS67
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
MES
Query on MES

Download Ideal Coordinates CCD File 
CA [auth E]
GA [auth F]
I [auth A]
K [auth B]
LA [auth G]
CA [auth E],
GA [auth F],
I [auth A],
K [auth B],
LA [auth G],
MA [auth H],
O [auth C],
W [auth D]
2-(N-MORPHOLINO)-ETHANESULFONIC ACID
C6 H13 N O4 S
SXGZJKUKBWWHRA-UHFFFAOYSA-N
EDO
Query on EDO

Download Ideal Coordinates CCD File 
AA [auth D]
BA [auth D]
DA [auth E]
EA [auth E]
FA [auth E]
AA [auth D],
BA [auth D],
DA [auth E],
EA [auth E],
FA [auth E],
HA [auth F],
IA [auth F],
J [auth A],
JA [auth F],
KA [auth F],
L [auth B],
M [auth B],
N [auth B],
NA [auth H],
OA [auth H],
P [auth C],
PA [auth H],
Q [auth C],
QA [auth H],
R [auth C],
RA [auth H],
S [auth C],
SA [auth H],
T [auth C],
TA [auth H],
U [auth C],
V [auth C],
X [auth D],
Y [auth D],
Z [auth D]
1,2-ETHANEDIOL
C2 H6 O2
LYCAIKOWRPUZTN-UHFFFAOYSA-N
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B, C, D, E
A, B, C, D, E, F, G, H
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.243 
  • R-Value Work: 0.193 
  • R-Value Observed: 0.196 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 60.523α = 89.35
b = 93.072β = 71.02
c = 93.397γ = 71.04
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-3000data reduction
HKL-3000data scaling
SHELXDphasing
MLPHAREphasing
DMphasing
RESOLVEphasing
HKL-3000phasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-09-02
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance