Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
homotrimer
-
pH 7.0, aggregation at pH 5.0, gel filtration, SDS-PAGE after chemical cross-linking
?
-
x * 73700, SDS-PAGE
?
-
x * 73700, SDS-PAGE
-
?
x * 114000, amino acid sequence calculation
?
-
x 82000, calculation from nucleotide sequence
?
x * 82000, amino acid sequence calculation
?
-
x * 47000 + x * 55000, HYAL3 in sperm, SDS-PAGE
?
-
x * 44000 + x * 47000, HYAL3 in sperm, SDS-PAGE
?
-
x * 120000, SDS-PAGE
-
?
x * 92000, amino acid sequence calculation
?
3 different form of 118, 111, and 92 kDa, the 118 kDa form is inactive
?
-
x * 100000, SDS-PAGE, x * 85000, SDS-PAGE, x * 75000-50000, trypsin digested enzyme, SDS-PAGE
?
x * 121000, amino acid sequence calculation
?
x * 107000, amino acid sequence calculation
?
x * 41000, N-terminal domain, SDS-PAGE, x * 41000, C-terminal domain, SDS-PAGE
?
x * 83208, mutant W292A, mass spectrometry, x * 83273, mutant F343V, mass spectrometry, x * 83097, mutant W291A/W292A, mass spectrometry, x * 83102, mutant W292A/F343V, mass spectrometry, x * 83027, mutant W291A/W292A/F343V, mass spectrometry
?
-
x * 40000, about, recombinant His6-tagged enzyme, SDS-PAGE
?
x * 54260, sequence calculation
monomer
1 * 80000, SDS-PAGE
monomer
x * 83218, calculation from nucleotide sequence
trimer
-
the enzyme belongs to PL subfamily 8, which has an overall alpha/alpha + beta architecture
trimer
-
3 * 36000-36900, SDS-PAGE and ESI-MS
trimer
3 * 40000, SDS-PAGE
additional information
enzyme is composed of 2 domains, alpha-helical alpha-domain and beta-sheet beta-domain, which are structurally and functionally distinct
additional information
-
enzyme is composed of 2 domains, alpha-helical alpha-domain and beta-sheet beta-domain, which are structurally and functionally distinct
additional information
-
homology model from crystal structure
additional information
-
the enzyme contains a distorted (alpha/alpha)5-6 barrel composed of alpha-helices inside and out, substrate binding is facilitated by the predominantly positive and hydrophobic cleft located at the top of the wider end of the barrel nested among helices and interhelix loops, domain structure, overview
additional information
-
the three-dimensional enzyme structure contains a catalytic alpha-domain at the N-terminus and a C-terminal supportive cell-wall-anchoring beta-domain connected by a short peptide linker
additional information
three-dimensional structure analysis, active site structure and hydrophobic patch, structure-function relationship
additional information
-
three-dimensional structure analysis, active site structure and hydrophobic patch, structure-function relationship
additional information
enzyme consists of 2 structural domains, C-terminal and N-terminal, each of which folds and unfolds independent from the other due to lack of cooperative interactions between them, structure determination
additional information
-
enzyme consists of 2 structural domains, C-terminal and N-terminal, each of which folds and unfolds independent from the other due to lack of cooperative interactions between them, structure determination
additional information
-
N-terminal alpha- and C-terminal beta-domain structure determination, determination of interface residues, overview
additional information
structure analysis, active site structure and hydrophobic patch, structure-function relationship
additional information
-
structure analysis, active site structure and hydrophobic patch, structure-function relationship
additional information
the enzyme contains a distorted (alpha/alpha)5-6 barrel composed of alpha-helices inside and out, substrate binding is facilitated by the predominantly positive and hydrophobic cleft located at the top of the wider end of the barrel nested among helices and interhelix loops, domain structure, overview
additional information
-
the three-dimensional enzyme structure contains a catalytic alpha-domain at the N-terminus and a C-terminal supportive cell-wall-anchoring beta-domain connected by a short peptide linker
additional information
-
three-dimensional structure analysis, unfolding process using 1-4 M guanidinium hydrochloride, effects of unfolding on the structure, transitions, kinetics, overview
additional information
-
the enzyme is very short in sequence and different in structure compared to enzymes of other species
additional information
extended trimeric conformation, homology modeling using the crystal structure of HylP1 from Streptococcus pyogenes SF370 (PDB ID-2C3F) as a template, domain structure, overview
additional information
-
extended trimeric conformation, homology modeling using the crystal structure of HylP1 from Streptococcus pyogenes SF370 (PDB ID-2C3F) as a template, domain structure, overview
additional information
Streptomyces hyalurolyticus
-
domain structure, overview