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1j5s

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

    Title Crystal structure of uronate isomerase (TM0064) from Thermotoga maritima at 2.85 A resolution. Proteins 53 142-145 2003
    Site JCSG
    PDB Id 1j5s Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1179,TM0064, 83921
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method XRAY
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    Chains 3
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.81 Rfactor 0.234
    Waters
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    Solvent Content 55.94

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1j5s
    1. Structural and catalytic diversity within the amidohydrolase superfamily
    CM Seibert, FM Raushel - Biochemistry, 2005 - ACS Publications
     
    2. Locating the stabilizing residues in (_/_) 8 barrel proteins based on hydrophobicity, long_range interactions, and sequence conservation
    MM Gromiha, G Pujadas, C Magyar - Proteins: Structure, , 2004 - Wiley Online Library
     
    3. 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
     
    4. Uronate isomerase: a nonhydrolytic member of the amidohydrolase superfamily with an ambivalent requirement for a divalent metal ion
    LK Williams, T Nguyen, Y Li, TN Porter - Biochemistry, 2006 - ACS Publications
     
    5. 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
     
    6. 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
     
    7. Crystal structure of uronate isomerase (TM0064) from Thermotoga maritima at 2.85 resolution
    R Schwarzenbacher, JM Canaves - Proteins: Structure, , 2003 - Wiley Online Library
     
    8. Target selection and annotation for the structural genomics of the amidohydrolase and enolase superfamilies
    U Pieper, R Chiang, JJ Seffernick, SD Brown - Journal of structural and , 2009 - Springer
     
    9. Modeling the three_dimensional structure of H+_ATPase of Neurospora crassa
    O Radresa, K Ogata, S Wodak - European Journal of , 2002 - Wiley Online Library
     
    10. High-throughput protein production for X-ray crystallography and use of size exclusion chromatography to validate or refute computational biological unit predictions
    D McMullan, JM Canaves, K Quijano - Journal of structural and , 2005 - Springer
     
    11. Are structural biases at protein termini a signature of vectorial folding?
    A Laio, C Micheletti - PROTEINS: Structure, Function, and , 2006 - Wiley Online Library
     
    12. Exploring the environmental preference of weak interactions in (_/_) 8 barrel proteins
    S Chakkaravarthi, MM Babu - PROTEINS: , 2006 - Wiley Online Library
     
    13. Analysis of chameleon sequences by energy decomposition on a pairwise per-residue basis
    S Yoon, H Jung - The protein journal, 2006 - Springer
     
    14. Protein function prediction by matching 3d structural data
    CC Chen, JT Tu, PK Chang, BY Chen - Proceedings of , 2004 - cmlab.csie.ntu.edu.tw
     
    15. Dimensionality reduction in computational demarcation of protein tertiary structures
    RR Joshi, PR Panigrahi, RN Patil - Journal of Molecular Modeling, 2011 - Springer
     

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    Protein Summary

    The TM0064 gene of Thermotoga maritima encodes a predicted uronate isomerase (EC:5.3.1.12; COG:COG1904; PFAM:PF02614). This enzyme catalyses the reactions: D-glucuronate <=> D-fructuronate and D-galacturonate <=> D-tagaturonate.

     

    1j5s structure folds into a TIM beta/alpha-barrel (SCOP sunid:51350) with all-alpha subdomain inserted after the first strand. The all-alpha subdomain has a novel fold, unique for uronate isomerase-like family (SCOP sunid:75082) [Ref].

    Ligand Summary



    References

    Reviews

    References

     

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