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trimer
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3 * 11100, SDS-PAGE
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x * 28000, SDS-PAGE
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x * 20000-20370, recombinant His-tagged enzyme, SDS-PAGE and DNA sequence determination
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x * 19481, determination of amino acid sequence
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x * 25860, recombinant enzyme, SDS-PAGE
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x * 25860, recombinant enzyme, SDS-PAGE
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x * 25860, recombinant enzyme, SDS-PAGE
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?
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x * 25860, recombinant enzyme, SDS-PAGE
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dimer
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dimer
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2 * 15000, SDS-PAGE
dimer
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2 * 27000, SDS-PAGE
dimer
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2 * 28000, SDS-PAGE
dimer
2 * 25000, SDS-PAGE
dimer
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2 * 17000-20000, SDS-PAGE, gel filtration in guanidine hydrochloride, peptide mapping data suggest that the subunits are quite similar if not identical
dimer
x-ray crystallography
dimer
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2 * 23000, SDS-PAGE
dimer
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2 * 24200, SDS-PAGE
dimer
the enzyme forms dimers in solution and in the crystals
dimer
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2 * 24200, SDS-PAGE
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dimer
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the enzyme forms dimers in solution and in the crystals
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dimer
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1 * 20000 + 1 * 34000, SDS-PAGE
homodimer
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homodimer
2 * 19150, about, sequence calculation, 2 * 21000, His-tagged recombinant enzyme TtAPRT2, SDS-PAGE
homodimer
secondary structure analysis, at the N-terminal end of the polypeptide chain, the hood domain is located encompassing a beta-sheet made of two antiparallel beta-strands, beta1 and beta2, and a disordered fragment following the beta2 strand, extending to the alpha1 helix
homodimer
TtAPRT2 structure analysis and comparisons. The asymmetric unit of TtAPRT2 crystal (PDB ID 5ZGO) contains six subunit chains A-F that comprise three identical homodimers AB, CD, and EF, all residues from N- to C-termini are modeled completely in all the six subunits of 5ZGO. Active site architecture shows that TtAPRT2 is formed by three domains that are common in all type APRTs, overview
homodimer
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2 * 19150, about, sequence calculation, 2 * 21000, His-tagged recombinant enzyme TtAPRT2, SDS-PAGE
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homodimer
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TtAPRT2 structure analysis and comparisons. The asymmetric unit of TtAPRT2 crystal (PDB ID 5ZGO) contains six subunit chains A-F that comprise three identical homodimers AB, CD, and EF, all residues from N- to C-termini are modeled completely in all the six subunits of 5ZGO. Active site architecture shows that TtAPRT2 is formed by three domains that are common in all type APRTs, overview
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homodimer
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secondary structure analysis, at the N-terminal end of the polypeptide chain, the hood domain is located encompassing a beta-sheet made of two antiparallel beta-strands, beta1 and beta2, and a disordered fragment following the beta2 strand, extending to the alpha1 helix
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homodimer
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2 * 19150, about, sequence calculation, 2 * 21000, His-tagged recombinant enzyme TtAPRT2, SDS-PAGE
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homodimer
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TtAPRT2 structure analysis and comparisons. The asymmetric unit of TtAPRT2 crystal (PDB ID 5ZGO) contains six subunit chains A-F that comprise three identical homodimers AB, CD, and EF, all residues from N- to C-termini are modeled completely in all the six subunits of 5ZGO. Active site architecture shows that TtAPRT2 is formed by three domains that are common in all type APRTs, overview
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homodimer
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secondary structure analysis, at the N-terminal end of the polypeptide chain, the hood domain is located encompassing a beta-sheet made of two antiparallel beta-strands, beta1 and beta2, and a disordered fragment following the beta2 strand, extending to the alpha1 helix
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additional information
three-dimensional structure, subunit structure
additional information
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three-dimensional structure, subunit structure
additional information
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three-dimensional structure, dimeric
additional information
three-dimensional structure, apo-enzyme in complexes with AMP, adenine, sulfate, citrate, subunit model
additional information
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three-dimensional structure, apo-enzyme in complexes with AMP, adenine, sulfate, citrate, subunit model
additional information
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association of subunits in presence of 5-phospho-alpha-D-ribose 1-diphosphate
additional information
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three-dimensional structure, apo-enzyme in complexes with AMP, adenine, sulfate, citrate, subunit model
additional information
enzyme crystals belonging to the P21 spatial group contain six identical enzyme subunits per asymmetric unit. Subunits are connected with a double axis pairwise and form three dimers (AB, CD, and EF). The polypeptide chain of a TthHB27APRT subunit contains 178 amino acid residues forming ten beta strands and four alpha helices. Enzyme structure analysis and comparisons, e.g. with APRT of TthHB8, overview
additional information
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enzyme crystals belonging to the P21 spatial group contain six identical enzyme subunits per asymmetric unit. Subunits are connected with a double axis pairwise and form three dimers (AB, CD, and EF). The polypeptide chain of a TthHB27APRT subunit contains 178 amino acid residues forming ten beta strands and four alpha helices. Enzyme structure analysis and comparisons, e.g. with APRT of TthHB8, overview
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additional information
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enzyme crystals belonging to the P21 spatial group contain six identical enzyme subunits per asymmetric unit. Subunits are connected with a double axis pairwise and form three dimers (AB, CD, and EF). The polypeptide chain of a TthHB27APRT subunit contains 178 amino acid residues forming ten beta strands and four alpha helices. Enzyme structure analysis and comparisons, e.g. with APRT of TthHB8, overview
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