2P8E

Crystal structure of the serine/threonine phosphatase domain of human PPM1B


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.82 Å
  • R-Value Free: 0.246 
  • R-Value Work: 0.186 
  • R-Value Observed: 0.189 

Starting Model: experimental
View more details

wwPDB Validation   3D Report Full Report


This is version 1.7 of the entry. See complete history


Literature

Structural genomics of protein phosphatases.

Almo, S.C.Bonanno, J.B.Sauder, J.M.Emtage, S.Dilorenzo, T.P.Malashkevich, V.Wasserman, S.R.Swaminathan, S.Eswaramoorthy, S.Agarwal, R.Kumaran, D.Madegowda, M.Ragumani, S.Patskovsky, Y.Alvarado, J.Ramagopal, U.A.Faber-Barata, J.Chance, M.R.Sali, A.Fiser, A.Zhang, Z.Y.Lawrence, D.S.Burley, S.K.

(2007) J Struct Funct Genomics 8: 121-140

  • DOI: https://doi.org/10.1007/s10969-007-9036-1
  • Primary Citation of Related Structures:  
    1RXD, 2FH7, 2G59, 2HCM, 2HHL, 2HXP, 2HY3, 2I0O, 2I1Y, 2I44, 2IQ1, 2IRM, 2ISN, 2NV5, 2OYC, 2P27, 2P4U, 2P69, 2P8E, 2PBN, 2Q5E, 2QJC, 2R0B

  • PubMed Abstract: 

    The New York SGX Research Center for Structural Genomics (NYSGXRC) of the NIGMS Protein Structure Initiative (PSI) has applied its high-throughput X-ray crystallographic structure determination platform to systematic studies of all human protein phosphatases and protein phosphatases from biomedically-relevant pathogens. To date, the NYSGXRC has determined structures of 21 distinct protein phosphatases: 14 from human, 2 from mouse, 2 from the pathogen Toxoplasma gondii, 1 from Trypanosoma brucei, the parasite responsible for African sleeping sickness, and 2 from the principal mosquito vector of malaria in Africa, Anopheles gambiae. These structures provide insights into both normal and pathophysiologic processes, including transcriptional regulation, regulation of major signaling pathways, neural development, and type 1 diabetes. In conjunction with the contributions of other international structural genomics consortia, these efforts promise to provide an unprecedented database and materials repository for structure-guided experimental and computational discovery of inhibitors for all classes of protein phosphatases.


  • Organizational Affiliation

    Albert Einstein College of Medicine, Bronx, NY, USA. [email protected]


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PPM1B beta isoform variant 6
A, B
307Homo sapiensMutation(s): 0 
Gene Names: PPM1B
EC: 3.1.3.16
UniProt & NIH Common Fund Data Resources
Find proteins for O75688 (Homo sapiens)
Explore O75688 
Go to UniProtKB:  O75688
PHAROS:  O75688
GTEx:  ENSG00000138032 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO75688
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
OCS
Query on OCS
A, B
L-PEPTIDE LINKINGC3 H7 N O5 SCYS
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.82 Å
  • R-Value Free: 0.246 
  • R-Value Work: 0.186 
  • R-Value Observed: 0.189 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 52.399α = 90
b = 92.315β = 90
c = 118.713γ = 90
Software Package:
Software NamePurpose
SCALAdata scaling
REFMACrefinement
PDB_EXTRACTdata extraction
MAR345data collection
MOSFLMdata reduction
CCP4data scaling
AMoREphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2007-04-03
    Type: Initial release
  • Version 1.1: 2007-10-16
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-10-18
    Changes: Refinement description
  • Version 1.4: 2018-11-14
    Changes: Data collection, Structure summary
  • Version 1.5: 2021-02-03
    Changes: Database references, Derived calculations, Structure summary
  • Version 1.6: 2023-08-30
    Changes: Data collection, Database references, Refinement description
  • Version 1.7: 2023-11-15
    Changes: Data collection