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Crystal structure of leech anti-platelet protein
Analyse Crystal structure of leech anti-platelet protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1I8N
- Type
- protein
- Length
- 267 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-platelet protein
- UniProt
- Q01747
- Ligands
- ROP
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Anti-platelet protein | protein | 89 | 18% helix, 36% strand | Q01747 |
Ligands and binding sites
- ROP · Propionamide · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 379 | 0.62 | 0.78 | 45 | empty |
| 2 | 111 | 0.57 | 0.84 | 29 | ROP |
| 3 | 120 | 0.56 | 0.84 | 23 | ROP |
Interfaces
2 interfaces between chains.
- A–C · 677 Ų buried · 21 hydrogen bonds · protein-protein
- A–B · 539 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 disulfide (disulfide).
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 Q01747
- Elsewhere: RCSB PDB 1I8N · PDBe 1I8N · UniProt Q01747
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