Research workbench
Solution structure of double super helix model
Analyse Solution structure of double super helix model in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3K2S
- Type
- protein
- Length
- 486 residues
- Chains
- 2
- Method
- solution scattering
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Apolipoprotein a-I
- UniProt
- P02647
- Ligands
- POV, CLR
- Pockets
- 2 · best druggability 0.30
Structure
solution scattering · 1 distinct chain · 62% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Apolipoprotein a-I | protein | 243 | 62% helix, 0% strand | P02647 |
Ligands and binding sites
- POV · (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate · ligand · 200 copies · chains A, B
- CLR · Cholesterol · ligand · 20 copies · chains A, B
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 | 65 | 0.30 | 0.74 | 13 | empty |
| 2 | 52 | 0.24 | 0.72 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 4425 Ų buried · 78 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 P02647
- Elsewhere: RCSB PDB 3K2S · PDBe 3K2S · UniProt P02647
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