5TW9

1.50 Angstrom Crystal Structure of C-terminal Fragment (residues 322-384) of Iron Uptake System Component EfeO from Yersinia pestis.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Free: 0.203 
  • R-Value Work: 0.173 
  • R-Value Observed: 0.174 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

1.50 Angstrom Crystal Structure of C-terminal Fragment (residues 322-384) of Iron Uptake System Component EfeO from Yersinia pestis.

Minasov, G.Shuvalova, L.Flores, K.Dubrovska, I.Grimshaw, S.Kwon, K.Anderson, W.F.Center for Structural Genomics of Infectious Diseases (CSGID)

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Iron uptake system component EfeO
A, B, C, D, E
A, B, C, D, E, F
63Yersinia pestisMutation(s): 0 
Gene Names: efeOYPO1855y2451YP_1538
UniProt
Find proteins for Q0WFT9 (Yersinia pestis)
Explore Q0WFT9 
Go to UniProtKB:  Q0WFT9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ0WFT9
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
IOD
Query on IOD

Download Ideal Coordinates CCD File 
G [auth A]
I [auth B]
J [auth B]
K [auth B]
L [auth C]
G [auth A],
I [auth B],
J [auth B],
K [auth B],
L [auth C],
M [auth C],
N [auth C],
O [auth C],
P [auth C],
Q [auth D],
R [auth D],
S [auth D],
T [auth D],
U [auth D],
W [auth E],
Y [auth F],
Z [auth F]
IODIDE ION
I
XMBWDFGMSWQBCA-UHFFFAOYSA-M
EDO
Query on EDO

Download Ideal Coordinates CCD File 
AA [auth F],
H [auth A],
V [auth D],
X [auth E]
1,2-ETHANEDIOL
C2 H6 O2
LYCAIKOWRPUZTN-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 34.037α = 90
b = 64.001β = 90
c = 173.151γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-3000data reduction
HKL-3000data scaling
PHENIXphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2016-11-30
    Type: Initial release
  • Version 1.1: 2024-03-06
    Changes: Data collection, Database references, Structure summary