5Q02

Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 1-(5-bromo-1,3-thiazol-2-yl)-3-[5-(1,2-oxazol-3-yl)thiophen-2-yl]sulfonylurea


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.095 Å
  • R-Value Free: 0.195 
  • R-Value Work: 0.149 

wwPDB Validation 3D Report Full Report


This is version 1.1 of the entry. See complete history

Literature

Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 1-(5-bromo-1,3-thiazol-2-yl)-3-[5-(1,2-oxazol-3-yl)thiophen-2-yl]sulfonylurea

Ruf, A.Joseph, C.Alker, A.Banner, D.Tetaz, T.Benz, J.Kuhn, B.Rudolph, M.

To be published.

Macromolecules

Find similar proteins by: Sequence  |  Structure

Entity ID: 1
MoleculeChainsSequence LengthOrganismDetails
Fructose-1,6-bisphosphatase 1
A, B, C, D
338Homo sapiensMutation(s): 0 
Gene Names: FBP1
Find proteins for Q2TU34 (Homo sapiens)
Go to Gene View: FBP1
Go to UniProtKB:  Q2TU34
Small Molecules
Ligands 1 Unique
IDChainsName / Formula / InChI Key2D Diagram3D Interactions
95J
Query on 95J

Download SDF File 
Download CCD File 
A, B, C, D
N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-5-(1,2-oxazol-3-yl)thiophene-2-sulfonamide
C11 H7 Br N4 O4 S3
QQPBXFNELFKWEI-UHFFFAOYSA-N
 Ligand Interaction
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.095 Å
  • R-Value Free: 0.195 
  • R-Value Work: 0.149 
  • Space Group: P 21 21 21
Unit Cell:
Length (Å)Angle (°)
a = 67.203α = 90.00
b = 83.311β = 90.00
c = 278.006γ = 90.00
Software Package:
Software NamePurpose
PHENIXrefinement
PDB_EXTRACTdata extraction

Structure Validation

View Full Validation Report or Ramachandran Plots



Entry History 

Deposition Data

Revision History 

  • Version 1.0: 2019-01-09
    Type: Initial release
  • Version 1.1: 2019-01-16
    Type: Data collection