4OMC

X-ray structure of human furin in complex with the competitive inhibitor meta-guanidinomethyl-Phac-RVR-Amba


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.216 
  • R-Value Work: 0.185 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

X-ray Structures of Human Furin in Complex with Competitive Inhibitors.

Dahms, S.O.Hardes, K.Becker, G.L.Steinmetzer, T.Brandstetter, H.Than, M.E.

(2014) ACS Chem Biol 9: 1113-1118

  • DOI: https://doi.org/10.1021/cb500087x
  • Primary Citation of Related Structures:  
    4OMC, 4OMD

  • PubMed Abstract: 

    Furin inhibitors are promising therapeutics for the treatment of cancer and numerous infections caused by bacteria and viruses, including the highly lethal Bacillus anthracis or the pandemic influenza virus. Development and improvement of inhibitors for pharmacological use require a detailed knowledge of the protease's substrate and inhibitor binding properties. Here we present a novel preparation of human furin and the first crystal structures of this enzyme in complex with noncovalent inhibitors. We show the inhibitor exchange by soaking, allowing the investigation of additional inhibitors and substrate analogues. Thus, our work provides a basis for the rational design of furin inhibitors.


  • Organizational Affiliation

    Protein Crystallography Group, Leibniz Institute for Age Research-Fritz Lipmann Institute (FLI) , Beutenbergstr. 11, 07745 Jena, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Furin
A, B, C, D, E
A, B, C, D, E, F
482Homo sapiensMutation(s): 0 
Gene Names: FURFURINPACEPCSK3
EC: 3.4.21.75
UniProt & NIH Common Fund Data Resources
Find proteins for P09958 (Homo sapiens)
Explore P09958 
Go to UniProtKB:  P09958
PHAROS:  P09958
GTEx:  ENSG00000140564 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP09958
Sequence Annotations
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  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
meta-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)benzamidine5N/AMutation(s): 0 
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
FMT
Query on FMT

Download Ideal Coordinates CCD File 
AB [auth F]
BB [auth F]
CA [auth C]
CB [auth F]
DA [auth C]
AB [auth F],
BB [auth F],
CA [auth C],
CB [auth F],
DA [auth C],
DB [auth F],
EA [auth C],
FA [auth C],
KA [auth D],
LA [auth D],
M [auth A],
MA [auth D],
N [auth A],
NA [auth D],
O [auth A],
P [auth A],
SA [auth E],
TA [auth E],
U [auth B],
UA [auth E],
V [auth B],
VA [auth E],
W [auth B],
X [auth B]
FORMIC ACID
C H2 O2
BDAGIHXWWSANSR-UHFFFAOYSA-N
CA
Query on CA

Download Ideal Coordinates CCD File 
AA [auth B]
EB [auth F]
FB [auth F]
GA [auth C]
GB [auth F]
AA [auth B],
EB [auth F],
FB [auth F],
GA [auth C],
GB [auth F],
HA [auth C],
IA [auth C],
OA [auth D],
PA [auth D],
Q [auth A],
QA [auth D],
R [auth A],
S [auth A],
WA [auth E],
XA [auth E],
Y [auth B],
YA [auth E],
Z [auth B]
CALCIUM ION
Ca
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
NA
Query on NA

Download Ideal Coordinates CCD File 
BA [auth B]
HB [auth F]
JA [auth C]
RA [auth D]
T [auth A]
BA [auth B],
HB [auth F],
JA [auth C],
RA [auth D],
T [auth A],
ZA [auth E]
SODIUM ION
Na
FKNQFGJONOIPTF-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.216 
  • R-Value Work: 0.185 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 141.178α = 90
b = 152.849β = 90
c = 168.306γ = 90
Software Package:
Software NamePurpose
MxCuBEdata collection
PHASERphasing
CNSrefinement
XDSdata reduction
XDSdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-04-09
    Type: Initial release
  • Version 1.1: 2014-05-28
    Changes: Database references