The Open Protein Structure Annotation Network
PDB Keyword


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

    Title Crystal structure of uncharacterized cystatin fold protein (YP_497570.1) from NTF2 superfamily (YP_497570.1) from NOVOSPHINGOBIUM AROMATICIVORANS DSM 12444 at 1.90 A resolution. To be published
    Site JCSG
    PDB Id 3ff2 Target Id 391039
    Molecular Characteristics
    Source Novosphingobium aromaticivorans dsm 12444
    Alias Ids TPS20870,SARO_25NOV03_CONTIG26_REVISED_GENE949, 3.10.450.50, 325195 Molecular Weight 12810.56 Da.
    Residues 116 Isoelectric Point 4.81
    Sequence lsnletakamiaaynaqdvdtyvsymtddaceanyrgdvvregkegtrsglaaafarwpqnhaeikdaq qvgtyvlmrehvtrgpatdgsplvepfdvvavysfegdkcsrvefir
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.90 Rfree 0.230
    Matthews' coefficent 3.50 Rfactor 0.187
    Waters 200 Solvent Content 64.86

    Ligand Information



    Protein Summary

    The Saro_2299 gene encodes for the protein YP_497570 from the SnoaL-like polyketide cyclase family (PF07366). The Conserved Domain Database indicates that it belongs to CD00531(NTF2_like) superfamily. Structural homologs of 3ff2 by Dali are hypothetical proteins and many ketosteroid isomerases (PDB:1qjg and PDB:8cho, etc). The superposition of 3ff2 with 1qjg is shown below. Although they are superimposed well (2.0A rmsd, 109 aligned, 17% id), three major catalytic residues (Tyr14, Asp38 and Asp99) of ketosteroid isomerase are not conserved in 3ff2.




    Fig. 1 Superposition of  3ff2 (green) with 1qjg (yellow).


    Although 391039 contains a monomer in the crystallographic asymmetric unit, the biomolecule of 3ff2 has been suggested as a dimer according to the calculation of interface interaction(PISA).


    Fig 1.  Biological molecule of 3ff2


    Cho, H.S.,  Ha, N.C.,  Choi, G.,  Kim, H.J.,  Lee, D.,  Oh, K.S.,  Kim, K.S.,  Lee, W.,  Choi, K.Y.,  Oh, B.H. (1999) Crystal structure of delta(5)-3-ketosteroid isomerase from Pseudomonas testosteroni in complex with equilenin settles the correct hydrogen bonding scheme for transition state stabilization. J.Biol.Chem. 274: 32863-32868

    Cho, H.S.,  Choi, G.,  Choi, K.Y.,  Oh, B.H.   (1998) Crystal structure and enzyme mechanism of Delta 5-3-ketosteroid isomerase from Pseudomonas testosteroni.  Biochemistry   37: 8325-8330  - 8cho (ligands: p4c)

    Ligand Summary

    An Acetate (ACT) from crystallization condition is found.




    No references found.

    Tag page
    • No tags

    Files (2)

    FileSizeDateAttached by 
    No description
    214.52 kB22:04, 19 Nov 2008gyewonActions
    No description
    178.08 kB03:37, 20 Nov 2008gyewonActions
    You must login to post a comment.
    All content on this site is licensed under a Creative Commons Attribution 3.0 License
    Powered by MindTouch