2AJL

X-ray Structure of Novel Biaryl-Based Dipeptidyl peptidase IV inhibitor


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.303 
  • R-Value Work: 0.226 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history


Literature

Discovery, SAR, and X-ray structure of novel biaryl-based dipeptidyl peptidase IV inhibitors

Qiao, L.Baumann, C.A.Crysler, C.S.Ninan, N.S.Abad, M.C.Spurlino, J.C.Desjarlais, R.L.Kervinen, J.Neeper, M.P.Bayoumy, S.S.Williams, R.Deckman, I.C.Dasgupta, M.Reed, R.L.Huebert, N.D.Tomczuk, B.E.Moriarty, K.J.

(2006) Bioorg Med Chem Lett 16: 123-128

  • DOI: https://doi.org/10.1016/j.bmcl.2005.09.037
  • Primary Citation of Related Structures:  
    2AJL

  • PubMed Abstract: 

    The discovery, SAR, and X-ray crystal structure of novel biarylaminoacyl-(S)-2-cyano-pyrrolidines and biarylaminoacylthiazolidines as potent inhibitors of dipeptidyl peptidase IV (DPP IV) are reported.


  • Organizational Affiliation

    Johnson and Johnson Pharmaceutical Research and Development, 665 Stockton Drive, Exton, PA 19341, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Dipeptidyl peptidase 4A [auth I],
B [auth J]
728Homo sapiensMutation(s): 0 
Gene Names: DPP4ADCP2CD26
EC: 3.4.14.5
UniProt & NIH Common Fund Data Resources
Find proteins for P27487 (Homo sapiens)
Explore P27487 
Go to UniProtKB:  P27487
PHAROS:  P27487
GTEx:  ENSG00000197635 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP27487
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
JNH
Query on JNH

Download Ideal Coordinates CCD File 
H [auth I],
R [auth J]
1-[2-(S)-AMINO-3-BIPHENYL-4-YL-PROPIONYL]-PYRROLIDINE-2-(S)-CARBONITRILE
C20 H25 N3 O
MUUVLSCVDXKQQV-OALUTQOASA-N
NAG
Query on NAG

Download Ideal Coordinates CCD File 
C [auth I]
D [auth I]
E [auth I]
F [auth I]
G [auth I]
C [auth I],
D [auth I],
E [auth I],
F [auth I],
G [auth I],
I [auth J],
J,
K [auth J],
L [auth J],
M [auth J],
N [auth J],
O [auth J],
P [auth J],
Q [auth J]
2-acetamido-2-deoxy-beta-D-glucopyranose
C8 H15 N O6
OVRNDRQMDRJTHS-FMDGEEDCSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
JNH PDBBind:  2AJL Ki: 13 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.303 
  • R-Value Work: 0.226 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 65.279α = 90
b = 126.877β = 99.41
c = 110.828γ = 90
Software Package:
Software NamePurpose
PROTEUM PLUSdata collection
PROTEUM PLUSdata reduction
CNSrefinement
PROTEUM PLUSdata scaling
CNSphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-11-08
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Non-polymer description, Version format compliance
  • Version 1.3: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Advisory, Data collection, Derived calculations, Structure summary
  • Version 1.4: 2023-08-23
    Changes: Data collection, Database references, Refinement description, Structure summary