Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.2.1.8 extracted from

  • Ulrich, A.; Wahl, M.C.
    Structure and evolution of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27 (2014), Acta Crystallogr. Sect. D, 70, 3110-3123 .
    View publication on PubMed
Search for more literature for 5.2.1.8

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens
expression in Escherichia coli Thermochaetoides thermophila

Crystallization (Commentary)

Crystallization (Comment) Organism
1.3 A resolution crystal structure of the peptidyl-prolyl cis-trans isomerase domain Thermochaetoides thermophila
structure of a relatively protease-resistant N-terminal fragment containing the PPIase domain, t 2.0 A resolution. Residues Arg56, Phe61, Ile62, Gln64, Ala102, Asn103, Phe114, Glu122, Leu123 and His127 in beta-strands 3, 4 and 6, as well as in the extended loop connecting beta-strands 6 and 7, form the proline-binding pocket Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
spliceosome complex
-
 Homo sapiens
-
-
spliceosome complex
-
 Thermochaetoides thermophila
-
-

Organism

Organism UniProt Comment Textmining
Homo sapiens Q6UX04
-
-
Thermochaetoides thermophila G0RY38
-
-
Thermochaetoides thermophila DSM 1495 G0RY38
-
-

Subunits

Subunits Comment Organism
? x * 53800, calculated for full-length protein, x * 17000, N-terminal fragment Homo sapiens

Synonyms

Synonyms Comment Organism
CTHT_0005290
-
 Thermochaetoides thermophila
Cwc27
-
 Homo sapiens
Cwc27
-
 Thermochaetoides thermophila
spliceosome-associated protein CWC27 homolog
-
 Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
48
-
 melting temperature, peptidyl-prolyl cis-trans isomerase domain Homo sapiens
51
-
 melting temperature, peptidyl-prolyl cis-trans isomerase domain Thermochaetoides thermophila