2Z7L

Unphosphorylated Mitogen Activated Protein Kinase ERK2 in Complex with (4-{[5-Carbamoyl-4-(3-Methylanilino)Pyrimidin 2-Yl]Amino}Phenyl)Acetic Acid

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.41 Å
  • R-Value Free: 0.276 
  • R-Value Work: 0.223 

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This is version 1.2 of the entry. See complete history. 


Literature

Identification of a key element for hydrogen-bonding patterns between protein kinases and their inhibitors

Katayama, N., Orita, M., Yamaguchi, T., Hisamichi, H., Kuromitsu, S., Kurihara, H., Sakashita, H., Matsumoto, Y., Fujita, S., Niimi, T.

(2008) Proteins 73: 795-801

  • DOI: https://doi.org/10.1002/prot.22207
  • Primary Citation of Related Structures:  
    2Z7L, 2Z8C

  • PubMed Abstract: 

    In this article, we report crystal structures for inhibitor-kinase complexes in which the inhibitor has different binding orientations and hydrogen-bonding patterns with extracellular-signal regulated kinase 2 and insulin receptor tyrosine kinase. Our crystallographic studies, and sequence and structural analyses of 532 coordinates of kinases held in the Protein Data Bank, suggest that the length of the "specificity linker" described here is a key structural element of the hydrogen-bonding patterns between protein kinases and their inhibitors.

    • Organizational Affiliation: 

    Drug Discovery Research, Astellas Pharma Inc., 21 Miyukigaoka, Tsukuba, Ibaraki 305-8585, Japan.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Mitogen-activated protein kinase 1366Rattus norvegicusMutation(s): 0 
Gene Names: Mapk1, Erk2, Mapk, Prkm1
EC: 2.7.11.24
UniProt
Find proteins for P63086 (Rattus norvegicus)
Explore P63086 
Go to UniProtKB:  P63086
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP63086
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.41 Å
  • R-Value Free: 0.276 
  • R-Value Work: 0.223 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 48.873α = 90
b = 69.962β = 109.58
c = 60.775γ = 90
Software Package:
Software NamePurpose
CNXrefinement
MOSFLMdata reduction
SCALAdata scaling
CNXphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-08-12
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-11-01
    Changes: Data collection, Database references, Derived calculations, Refinement description