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

    Title Crystal structure of putative phosphosugar isomerase (NP_459564.1) from SALMONELLA TYPHIMURIUM LT2 at 2.12 A resolution. To be published
    Site JCSG
    PDB Id 3fkj Target Id 391508
    Molecular Characteristics
    Source Salmonella typhimurium lt2
    Alias Ids TPS20899,NP_459564.1,, 384243 Molecular Weight 36725.60 Da.
    Residues 328 Isoelectric Point 5.33
    Sequence msvahenarriisdilgkqniervwfvgcggsltgfwpgkyfldceasklavgyitsnefvhatpkalg knsvvilasqqgntaetvaaarvarekgaatiglvyqpdtplceysdyiieyqwarypetvdpaqqkaa yslwlaleilaqtegyaqydelvsafgrfsdvvhgaqrqvqedaqrfaaewkdekvvymmgsgpsfgaa hqesicillemqwinsasihsgeyfhgpfeitepgtpfillqssgrtrplddrairfieryqgklqlid adklgiqdlstdvgeyfcgllhncvldvynlalatarnhplttrrymwkvey
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 2.12 Rfree 0.212
    Matthews' coefficent 2.21 Rfactor 0.165
    Waters 316 Solvent Content 44.45

    Ligand Information


    Google Scholar output for 3fkj
    1. Exchanging a single amino acid residue generates or weakens a+ 2 cellooligosaccharide binding subsite in rice _-glucosidases
    S Sansenya, J Maneesan, JR Ketudat Cairns - Carbohydrate Research, 2012 - Elsevier

    Protein Summary

    Gene STM_0572 from Salmonella typhimurium lt2 encodes the NP_459564 protein that contains a tandem repeat of the SIS domain (PF01380).  Genome context analysis using the STRING server predicsts that STM_0572 is functionally associated with enzymes from fructose and mannose metabolism.

    Pre-SCOP classifies 3fkj in the alpha/beta class, SIS domain superfamily, double SIS domain family (PFAM PF01380.15 SIS CL0067). 3fkj structure is similar to jcsg structure 3eua (seq id 38%, rmsd 1.3A for 319 aligned Ca atoms; Dali Z=45). The active site residues are conserved between these two proteins, thus most likely they share the same function as sugar isomerases.

    Significant structural similarity is also found with a glucosamine 6-phosphate synthase (GlmS) with bound ligand alpha-D-glucose-6-phosphate (G6P), PDB:1mor [Ref]. Structure comparison with TopMatch (273 equivalent residues, 2.15Å rmsd, 19% sequence identity) of the two protein chains reveals a highly conserved phosphate binding loop consisting of equivalent residues Ser-32/303, Ser-78/347, Gln-79/348 and further high conservation up to residue Gly-97/366 (3fkj/1mor). Furthermore, residues believed to be catalytic in 1mor (Lys-603, a Schiff base;  His-504, the ring-opening step; Glu-488, the proton transfer from C1 to C2 of the substrate G6P) are conserved. On the other hand, a distinct C-terminal motif for GlmS, DXPXXLAK[SC]VT, is not found in 3fkj.

    Figure 1. Dimeric crystal structure of 3fkj


    Figure 2. 3fkj dimer structure (red) superimposed to 3eua (cyan)


    Figure 3. The putative active site of 3fkj is defined by a deep groove near the dimer interface


    Ligand Summary




    1. (No Results)


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    Files (3)

    FileSizeDateAttached by 
    dimer (red) comparison with vs 3eua
    178.47 kB23:41, 4 Dec 2008qxuActions
    dimer of 391508
    166.29 kB23:25, 4 Dec 2008qxuActions
    active site of 391508
    202.01 kB23:47, 4 Dec 2008qxuActions
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