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Crystal structure and expression patterns of prolyl 4-hydroxylases from Phytophthora capsici
Analyse Crystal structure and expression patterns of prolyl 4-hydroxylases from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IUQ
- Type
- protein
- Length
- 591 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.348
- Source
- Phytophthora capsici LT1534
- Molecule
- Prolyl 4-hydroxylase
- Ligands
- FE2
- Pockets
- 9 · best druggability 0.75
Structure
x-ray diffraction · resolution 2.348 · 2 distinct chains · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prolyl 4-hydroxylase | protein | 295 | 44% helix, 20% strand | — |
| B | Prolyl 4-hydroxylase | protein | 296 | 44% helix, 20% strand | — |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 67 | 0.75 | 0.98 | 21 | empty |
| 2 | 59 | 0.72 | 0.98 | 22 | empty |
| 3 | 229 | 0.57 | 0.79 | 26 | empty |
| 4 | 165 | 0.55 | 0.80 | 23 | FE2 |
| 5 | 188 | 0.54 | 0.79 | 25 | FE2 |
Interfaces
1 interface between chains.
- A–B · 441 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified, 2 disulfide (engineered, disulfide).
Compared structures
- 6IUQ · Crystal structure and expression patterns of prolyl 4-hydroxylases from phytophthora… · 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
- Elsewhere: RCSB PDB 6IUQ · PDBe 6IUQ
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