Research workbench
Trans-3/4-proline-hydroxylase H11 with 4-hydroxyl-proline
Analyse Trans-3/4-proline-hydroxylase H11 with 4-hydroxyl-proline in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E08
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phytanoyl-CoA dioxygenase
- UniProt
- S5TUM1
- Ligands
- HYP
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phytanoyl-CoA dioxygenase | protein | 263 | 28% helix, 22% strand | S5TUM1 |
Ligands and binding sites
- HYP · 4-hydroxyproline · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.78 | 0.96 | 32 | HYP |
| 2 | 108 | 0.43 | 0.77 | 12 | empty |
| 3 | 65 | 0.34 | 0.76 | 12 | empty |
Compared structures
- 7E08 · Trans-3/4-proline-hydroxylase H11 with 4-Hydroxyl-proline · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt S5TUM1
- Elsewhere: RCSB PDB 7E08 · PDBe 7E08 · UniProt S5TUM1
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