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octamer
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8 * 50000, about
?
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x * 44500, recombinant enzyme, SDS-PAGE
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x * 44500, recombinant His-tagged wild-type and mutant LAPII, SDS-PAGE
?
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x * 61000, recombinant chimeric enzyme, SDS-PAGE
?
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x * 47000 + x * 50000
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x * 44000-46300, unprocessed periplasmic enzyme, SDS-PAGE, x * 31000-32000, processed extracellular and periplasmic enzyme, SDS-PAGE, x * 39000-40000, unprocessed extracellular enzyme, SDS-PAGE,x * 51000-52000, unprocessed recombinant enzyme, SDS-PAGE
?
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x * 51000, recombinant His-tagged enzyme, SDS-PAGE
dodecamer
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12 * 18000
hexamer
6 * 50000, SDS-PAGE
hexamer
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6 * 54879, structure analysis and sequence calculation, three-dimensional structure modelling with C-terminal catalytic domain
hexamer
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lens enzyme three-dimensional structure and protein fold, overview
hexamer
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crystal structure
hexamer
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6 * 55000, recombinant LAP, SDS-PAGE
hexamer
6 * 55000, recombinant enzyme, SDS-PAGE
hexamer
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6 * 55000, recombinant enzyme, SDS-PAGE
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monomer
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1 * 31000, SDS-PAGE
monomer
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1 * 46425, sequence calculation
monomer
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1 * 42977, mass spectrometry
monomer
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1 * 42977, mass spectrometry
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monomer
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1 * 30000-32000, mature active enzyme
oligomer
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x * 14000, API, SDS-PAGE, x * 18000, APII, SDS-PAGE
oligomer
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x * 14000, API, SDS-PAGE, x * 18000, APII, SDS-PAGE
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additional information
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three-dimensional structure analysis
additional information
oligomerization is required for activity, the monomer is inactive, the enzyme contains no disulfide bonds, peptide mass fingerprinting, overview
additional information
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polymer, but probably only due to artificial aggregation
additional information
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the monomeric enzyme is probably not active
additional information
the HpM17AP subunit consists of a single polypeptide chain of 496 residues and comprises a total of 14 alpha-helices and 16 beta-strands, which account for 39% and 15% of the total residues, respectively. Like other M17 aminopeptidases, HpM17AP folds into two domains of a mixed alpha/beta structure connected via a long helix alpha4. The N-terminal domain comprises residues 1 to 155, the connecting helix runs from residue 156 to 182 and the C-terminal domain comprises residues 183 to 496. Residues 97-103 and 147-154 are not included in the model due to poorly defined electron density. Topology of the secondary structure elements, overview
additional information
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the HpM17AP subunit consists of a single polypeptide chain of 496 residues and comprises a total of 14 alpha-helices and 16 beta-strands, which account for 39% and 15% of the total residues, respectively. Like other M17 aminopeptidases, HpM17AP folds into two domains of a mixed alpha/beta structure connected via a long helix alpha4. The N-terminal domain comprises residues 1 to 155, the connecting helix runs from residue 156 to 182 and the C-terminal domain comprises residues 183 to 496. Residues 97-103 and 147-154 are not included in the model due to poorly defined electron density. Topology of the secondary structure elements, overview
additional information
-
the HpM17AP subunit consists of a single polypeptide chain of 496 residues and comprises a total of 14 alpha-helices and 16 beta-strands, which account for 39% and 15% of the total residues, respectively. Like other M17 aminopeptidases, HpM17AP folds into two domains of a mixed alpha/beta structure connected via a long helix alpha4. The N-terminal domain comprises residues 1 to 155, the connecting helix runs from residue 156 to 182 and the C-terminal domain comprises residues 183 to 496. Residues 97-103 and 147-154 are not included in the model due to poorly defined electron density. Topology of the secondary structure elements, overview
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additional information
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the HpM17AP subunit consists of a single polypeptide chain of 496 residues and comprises a total of 14 alpha-helices and 16 beta-strands, which account for 39% and 15% of the total residues, respectively. Like other M17 aminopeptidases, HpM17AP folds into two domains of a mixed alpha/beta structure connected via a long helix alpha4. The N-terminal domain comprises residues 1 to 155, the connecting helix runs from residue 156 to 182 and the C-terminal domain comprises residues 183 to 496. Residues 97-103 and 147-154 are not included in the model due to poorly defined electron density. Topology of the secondary structure elements, overview
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additional information
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amino acid composition
additional information
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amino acid composition
additional information
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the proenzyme contains a 21-amino acid-signal peptide, and a 84-amino acid N-terminal propeptide, 299 amino acids form the mature protein part, and 100 amino acids form the C-terminal propeptide