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The Open Protein Structure Annotation Network
PDB Keyword
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1j6p

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title Crystal structure of Metal-dependent hydrolase of cytosinedemaniase/chlorohydrolase family (TM0936) from Thermotoga maritima at 1.9 A resolution. To be published
    Site JCSG
    PDB Id 1j6p Target Id 282805
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1248,TM0936, _0113.002264_, 84735, 90077 Molecular Weight 45770.12 Da.
    Residues 406 Isoelectric Point 5.15
    Sequence miignclilkdfssepfwgaveiengtikrvlqgevkvdldlsgklvmpalfnththapmtllrgvaed lsfeewlfskvlpiedrltekmayygtilaqmemarhgiagfvdmyfheewiakavrdfgmralltrgl vdsngddggrleenlklynewngfegrifvgfgphspylcseeylkrvfdtakslnapvtihlyetske eydledilniglkevktiaahcvhlperyfgvlkdipffvshnpasnlklgngiapvqrmiehgmkvtl gtdgaasnnslnlffemrlasllqkaqnprnldvntclkmvtydgaqamgfksgkieegwnadlvvidl dlpemfpvqniknhlvhafsgevfatmvagkwiyfdgeyptidseevkrelariekelyss
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.90 Rfree 0.202
    Matthews' coefficent 3.16 Rfactor 0.175
    Waters 174 Solvent Content 61.10

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    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1j6p
    1. Structure-based activity prediction for an enzyme of unknown function
    JC Hermann, R Marti-Arbona, AA Fedorov, E Fedorov - Nature, 2007 - nature.com
     
    2. Structural and catalytic diversity within the amidohydrolase superfamily
    CM Seibert, FM Raushel - Biochemistry, 2005 - ACS Publications
     
    3. Leveraging enzyme structure-function relationships for functional inference and experimental design: the structure-function linkage database
    SCH Pegg, SD Brown, S Ojha, J Seffernick - Biochemistry, 2006 - ACS Publications
     
    4. Annotating enzymes of unknown function: N-formimino-L-glutamate deiminase is a member of the amidohydrolase superfamily
    R Mart-Arbona, C Xu, S Steele, A Weeks, GF Kuty - Biochemistry, 2006 - ACS Publications
     
    5. At the periphery of the amidohydrolase superfamily: Bh0493 from Bacillus halodurans catalyzes the isomerization of D-galacturonate to D-tagaturonate
    TT Nguyen, S Brown, AA Fedorov, EV Fedorov - Biochemistry, 2008 - ACS Publications
     
    6. The Crystal Structure of a Novel, Latent Dihydroorotase from Aquifex aeolicus at 1.7 Resolution
    PD Martin, C Purcarea, P Zhang, A Vaishnav - Journal of molecular , 2005 - Elsevier
     
    7. Shotgun crystallization strategy for structural genomics II: crystallization conditions that produce high resolution structures for T. maritima proteins
    R Page, AM Deacon, SA Lesley - Journal of structural and , 2005 - Springer
     
    8. Efficient recognition of protein fold at low sequence identity by conservative application of Psi_BLAST: application
    FJ Stevens, C Kuemmel, G Babnigg - Journal of Molecular , 2005 - Wiley Online Library
     
    9. Catalytic improvement and evolution of atrazine chlorohydrolase
    C Scott, CJ Jackson, CW Coppin - Applied and , 2009 - Am Soc Microbiol
     
    10. Efficient recognition of protein fold at low sequence identity by conservative application of Psi_BLAST: validation
    FJ Stevens - Journal of Molecular Recognition, 2005 - Wiley Online Library
     
    11. The Enzyme Function Initiative
    JA Gerlt, KN Allen, SC Almo, RN Armstrong - Biochemistry, 2011 - ACS Publications
     

    Protein Summary

    TM0936 has a fold typical for a amidohydrolase superfamily (AHS), consisting of two domains, a TIM barrel and a beta roll.

    TM0936 is a S-adenosylhomocysteine (SAH) deaminase, part of a novel and as yet uncharacterized pathway of SAH degradation, as  recently demonstrated in Hermann JC, Marti-Arbona R, Fedorov AA, Fedorov E, Almo SC, Shoichet BK, Raushel FM.   "Structure-based activity prediction for an enzyme of unknown function." Nature. 2007 448:775-9

    Ligand Summary

    The JCSG structure was solved without a ligand. Subsequently, a complex of TM0936 with methionine (1p1m) was solved by the New York Structural GenomiX Research Consortium (NYSGXRC) and a complex with the product resulting from the deamination of SAH, S-inosylhomocysteine was solved by the Frank M. Raushel group at Texas A&M (2plm).

    References

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