Research workbench
Crystal structure of soluble epcr after exposure to the nonionic surfactant polysorbate 20
Analyse Crystal structure of soluble epcr after exposure to the nonionic surfactant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OKV
- Type
- protein
- Length
- 167 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endothelial protein C receptor
- UniProt
- Q9UNN8
- Ligands
- R16, D10, NAG
- Pockets
- 1 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endothelial protein C receptor | protein | 167 | 35% helix, 38% strand | Q9UNN8 |
Ligands and binding sites
- R16 · Hexadecane · ligand · chains A
- D10 · Decane · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
- HEX · Hexane · additive · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 595 | 0.81 | 0.86 | 61 | R16, HEX, D10 |
Modifications
Observed in the structure: 3 glycan (N-glycosylation).
Compared structures
- 7OKV · Crystal structure of soluble EPCR after exposure to the nonionic surfactant Polysorbate 20 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UNN8 · AlphaFold monomer V2.0 prediction for endothelial protein C receptor (Q9UNN8) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9UNN8
- Elsewhere: RCSB PDB 7OKV · PDBe 7OKV · UniProt Q9UNN8
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