CATH Classification
Level | CATH Code | Description |
---|---|---|
2 | Mainly Beta | |
2.40 | Beta Barrel | |
2.40.100 | Cyclophilin | |
2.40.100.10 | Cyclophilin-like |
Domain Context
CATH Clusters
Superfamily | Cyclophilin-like |
Functional Family | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type |
Enzyme Information
5.2.1.8 |
Peptidylprolyl isomerase.
based on mapping to UniProt Q13356
Peptidylproline (omega=180) = peptidylproline (omega=0).
-!- The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. -!- Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. -!- The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.
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2.3.2.27 |
RING-type E3 ubiquitin transferase.
based on mapping to UniProt Q13356
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.
-!- The RING domain of E3 ubiquitin transferase serves as a mediator bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin an the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- The RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin (unlike the HECT domain, EC 2.3.2.26). -!- RING-type ubiquitin transferases may occur as single-chain enzymes but also in dimeric forms or in multi-subunit assemblies. -!- Formerly EC 6.3.2.19 and EC 6.3.2.21.
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UniProtKB Entries (1)
Q13356 |
PPIL2_HUMAN
Homo sapiens
Peptidyl-prolyl cis-trans isomerase-like 2
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PDB Structure
PDB | 1ZKC |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases.
PLoS Biol.
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