Research workbench
Structure of platelet glycoprotein 1B alpha with a bound peptide inhibitor
Analyse Structure of platelet glycoprotein 1B alpha with a bound peptide inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3P72
- Type
- protein
- Length
- 280 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Platelet glycoprotein ib alpha chain; OS1 peptide
- UniProt
- P07359
- Ligands
- CL
- Pockets
- 2 · best druggability 0.35
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Platelet glycoprotein ib alpha chain | protein | 269 | 10% helix, 17% strand | P07359 |
| B | OS1 peptide | protein | 11 | 55% helix, 0% strand | — |
Ligands and binding sites
- CL · Chloride 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.35 | 0.79 | 18 | empty |
| 2 | 51 | 0.24 | 0.72 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 604 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3P72 · structure of platelet Glycoprotein 1b alpha with a bound peptide inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
- P07359 · AlphaFold monomer V2.0 prediction for platelet glycoprotein ib alpha chain (P07359) · 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 P07359
- Elsewhere: RCSB PDB 3P72 · PDBe 3P72 · UniProt P07359
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