MolNFT v1 · #47001 · protein
Crystal structure of the serine protease domain of prophenoloxidase activating factor-I in a zymogen form
2OLG · Pro-phenoloxidase activating enzyme-I: “Crystal structure of the serine protease domain of prophenoloxidase activating factor-I in a zymogen form”. X-ray diffraction, 3 ligands (NAG, CA, SO4), 2 pockets (best druggability 0.52).…
- PDB
- 2OLG
- Type
- protein
- Length
- 276 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pro-phenoloxidase activating enzyme-I
- UniProt
- O97366
- Ligands
- NAG, CA, SO4
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pro-phenoloxidase activating enzyme-I | protein | 276 | 11% helix, 32% strand | O97366 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
- CA · Calcium ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 154 | 0.52 | 0.80 | 30 | empty |
| 2 | 51 | 0.31 | 0.77 | 19 | empty |
Modifications
Observed in the structure: 5 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 2OLG · Crystal structure of the serine protease domain of prophenoloxidase activating factor-I… · the same entry in another collection · chain A against A, TM-score 1.00
- O97366 · AlphaFold monomer V2.0 prediction for phenoloxidase-activating factor 1 (O97366) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 O97366
- Elsewhere: RCSB PDB 2OLG · PDBe 2OLG · UniProt O97366
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