Research workbench
Proline 3-hydroxylase (type II) - iron form
Analyse Proline 3-hydroxylase (type II) - iron form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1E5S
- Type
- protein
- Length
- 503 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proline oxidase
- UniProt
- O09345
- Ligands
- FE2, SO4
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proline oxidase | protein | 260 | 27% helix, 24% strand | O09345 |
| B | Proline oxidase | protein | 243 | 32% helix, 22% strand | O09345 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 256 | 0.65 | 0.82 | 34 | empty |
| 2 | 284 | 0.65 | 0.81 | 40 | SO4, FE2 |
| 3 | 368 | 0.60 | 0.77 | 47 | empty |
| 4 | 120 | 0.43 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 387 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
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 O09345
- Elsewhere: RCSB PDB 1E5S · PDBe 1E5S · UniProt O09345
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