2CJF

TYPE II DEHYDROQUINASE INHIBITOR COMPLEX


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.334 
  • R-Value Work: 0.274 
  • R-Value Observed: 0.277 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history


Literature

Design, synthesis, and structural studies on potent biaryl inhibitors of type II dehydroquinases.

Payne, R.J.Riboldi-Tunnicliffe, A.Kerbarh, O.Abell, A.D.Lapthorn, A.J.Abell, C.

(2007) ChemMedChem 2: 1010-1013


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
3-DEHYDROQUINATE DEHYDRATASE
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J, K, L
157Streptomyces coelicolorMutation(s): 0 
EC: 4.2.1.10
UniProt
Find proteins for P15474 (Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145))
Explore P15474 
Go to UniProtKB:  P15474
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP15474
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 4 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
RP4
Query on RP4

Download Ideal Coordinates CCD File 
BA [auth G]
EA [auth H]
GA [auth I]
IA [auth J]
M [auth A]
BA [auth G],
EA [auth H],
GA [auth I],
IA [auth J],
M [auth A],
NA [auth K],
O [auth B],
QA [auth L],
S [auth C],
T [auth D],
W [auth E],
Y [auth F]
(1S,4S,5S)-1,4,5-TRIHYDROXY-3-[3-(PHENYLTHIO)PHENYL]CYCLOHEX-2-ENE-1-CARBOXYLIC ACID
C19 H18 O5 S
QMNMNSINKIFYBV-LMMKCTJWSA-N
TRS
Query on TRS

Download Ideal Coordinates CCD File 
HA [auth I],
KA [auth J],
Q [auth B],
U [auth D]
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
C4 H12 N O3
LENZDBCJOHFCAS-UHFFFAOYSA-O
PO4
Query on PO4

Download Ideal Coordinates CCD File 
CA [auth G],
JA [auth J],
P [auth B],
Z [auth F]
PHOSPHATE ION
O4 P
NBIIXXVUZAFLBC-UHFFFAOYSA-K
GOL
Query on GOL

Download Ideal Coordinates CCD File 
AA [auth F]
DA [auth G]
FA [auth H]
LA [auth J]
MA [auth J]
AA [auth F],
DA [auth G],
FA [auth H],
LA [auth J],
MA [auth J],
N [auth A],
OA [auth K],
PA [auth K],
R [auth B],
RA [auth L],
V [auth D],
X [auth E]
GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
RP4 Binding MOAD:  2CJF Ki: 380 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.334 
  • R-Value Work: 0.274 
  • R-Value Observed: 0.277 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 195.755α = 65.84
b = 195.73β = 65.89
c = 239.68γ = 89.97
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling
AMoREphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-04-10
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-05-08
    Changes: Data collection, Database references, Experimental preparation, Other
  • Version 1.4: 2023-12-13
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description