1CM8

PHOSPHORYLATED MAP KINASE P38-GAMMA

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.283 
  • R-Value Work: 0.232 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history. 


Literature

The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation.

Bellon, S., Fitzgibbon, M.J., Fox, T., Hsiao, H.M., Wilson, K.P.

(1999) Structure 7: 1057-1065

  • DOI: https://doi.org/10.1016/s0969-2126(99)80173-7
  • Primary Citation of Related Structures:  
    1CM8

  • PubMed Abstract: 

    Mitogen-activated protein (MAP) kinases mediate the cellular response to stimuli such as pro-inflammatory cytokines and environmental stress. P38gamma is a new member of the MAP kinase family, and is expressed at its highest levels in skeletal muscle. P38gamma is 63% identical in sequence to P38alpha. The structure of P38alpha MAP kinase has been determined in the apo, unphosphorylated, inactive form. The structures of apo unphosphorylated ERK2, a related MAP kinase, and apo phosphorylated ERK2 have also been determined.

    • Organizational Affiliation: 

    Vertex Pharmaceuticals Incorporated 130 Waverly Street, Cambridge, MA 02139-4211, USA. bellon@vpharm.com.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PHOSPHORYLATED MAP KINASE P38-GAMMA
A, B
367Homo sapiensMutation(s): 2 
UniProt & NIH Common Fund Data Resources
Find proteins for P53778 (Homo sapiens)
Explore P53778 
Go to UniProtKB:  P53778
PHAROS:  P53778
GTEx:  ENSG00000188130 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP53778
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  2 Unique
IDChains TypeFormula2D DiagramParent
PTR
Query on PTR
A, B
L-PEPTIDE LINKINGC9 H12 N O6 PTYR
TPO
Query on TPO
A, B
L-PEPTIDE LINKINGC4 H10 N O6 PTHR
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.283 
  • R-Value Work: 0.232 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 63.5α = 90
b = 66.82β = 90
c = 206.02γ = 90
Software Package:
Software NamePurpose
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-05-17
    Type: Initial release
  • Version 1.1: 2008-04-26
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-12-27
    Changes: Data collection, Database references, Derived calculations