CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.25 | Alpha Horseshoe |
|
1.25.40 | Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat |
|
1.25.40.10 | Tetratricopeptide repeat domain |
Domain Context
CATH Clusters
| Superfamily | Tetratricopeptide repeat domain |
| Functional Family | Prolyl 4-hydroxylase subunit alpha 2 |
Enzyme Information
| 1.14.11.2 |
Procollagen-proline 4-dioxygenase.
based on mapping to UniProt O15460
L-proline-[procollagen] + 2-oxoglutarate + O(2) = trans-4-hydroxy-L- proline-[procollagen] + succinate + CO(2).
-!- The enzyme, which is located within the lumen of the endoplasmic reticulum, catalyzes the 4-hydroxylation of prolines in -X-Pro-Gly- sequences. -!- The 4-hydroxyproline residues are essential for the formation of the collagen triple helix. -!- The enzyme forms a complex with protein disulfide isomerase and acts not only on procollagen but also on more than 15 other proteins that have collagen-like domains.
|
UniProtKB Entries (1)
| O15460 |
P4HA2_HUMAN
Homo sapiens
Prolyl 4-hydroxylase subunit alpha-2
|
PDB Structure
| PDB | 6EVO |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural enzymology binding studies of the peptide-substrate-binding domain of human collagen prolyl 4-hydroxylase (type-II): High affinity peptides have a PxGP sequence motif.
Protein Sci.
|
