CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
6 | Special |
|
6.10 | Helix non-globular |
|
6.10.140 | Helix Hairpins |
|
6.10.140.1460 |
Domain Context
CATH Clusters
| Superfamily | 6.10.140.1460 |
| Functional Family |
Enzyme Information
| 1.14.11.2 |
Procollagen-proline 4-dioxygenase.
based on mapping to UniProt P13674
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)
| P13674 |
P4HA1_HUMAN
Homo sapiens
Prolyl 4-hydroxylase subunit alpha-1
|
PDB Structure
| PDB | 2YQ8 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The Structural Motifs for Substrate Binding and Dimerization of the Alpha Subunit of Collagen Prolyl 4-Hydroxylase
Structure
|
