6DQO

Crystal structure of SsuE FMN reductase Y118A mutant in FMN bound form.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.705 Å
  • R-Value Free: 0.207 
  • R-Value Work: 0.184 

wwPDB Validation 3D Report Full Report


This is version 1.0 of the entry. See complete history

Literature

Not as easy as pi : An insertional residue does not explain the pi-helix gain-of-function in two-component FMN reductases.

McFarlane, J.S.Hagen, R.A.Chilton, A.S.Forbes, D.L.Lamb, A.L.Ellis, H.R.

(2019) Protein Sci. 28: 123-134


Macromolecules

Find similar proteins by: Sequence  |  Structure

Entity ID: 1
MoleculeChainsSequence LengthOrganismDetails
FMN reductase (NADPH)
A
191Escherichia coli (strain K12)Mutation(s): 1 
Gene Names: ssuE (ycbP)
EC: 1.5.1.38
Find proteins for P80644 (Escherichia coli (strain K12))
Go to UniProtKB:  P80644
Small Molecules
Ligands 2 Unique
IDChainsName / Formula / InChI Key2D Diagram3D Interactions
FMN
Query on FMN

Download SDF File 
Download CCD File 
A
FLAVIN MONONUCLEOTIDE
RIBOFLAVIN MONOPHOSPHATE
C17 H21 N4 O9 P
FVTCRASFADXXNN-SCRDCRAPSA-N
 Ligand Interaction
GOL
Query on GOL

Download SDF File 
Download CCD File 
A
GLYCEROL
GLYCERIN; PROPANE-1,2,3-TRIOL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
 Ligand Interaction
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.705 Å
  • R-Value Free: 0.207 
  • R-Value Work: 0.184 
  • Space Group: C 2 2 21
Unit Cell:
Length (Å)Angle (°)
a = 80.911α = 90.00
b = 110.847β = 90.00
c = 41.727γ = 90.00
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
AutoPROCdata scaling
PHASERphasing

Structure Validation

View Full Validation Report or Ramachandran Plots



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Science Foundation (United States)United StatesMCB-1244320
National Science Foundation (United States)United StatesCHE-1403293

Revision History 

  • Version 1.0: 2019-01-09
    Type: Initial release