Research workbench
Structure of the trimeric globular domain of adiponectin
Analyse Structure of the trimeric globular domain of adiponectin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6U66
- Type
- protein
- Length
- 415 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adiponectin
- UniProt
- Q15848
- Ligands
- CA, NA
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 0% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adiponectin | protein | 136 | 0% helix, 58% strand | Q15848 |
| B | Adiponectin | protein | 142 | 0% helix, 56% strand | Q15848 |
| C | Adiponectin | protein | 137 | 0% helix, 58% strand | Q15848 |
Ligands and binding sites
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 | 380 | 0.75 | 0.85 | 23 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1285 Ų buried · 28 hydrogen bonds · protein-protein
- B–C · 1250 Ų buried · 28 hydrogen bonds · protein-protein
- A–C · 1216 Ų buried · 28 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 Q15848
- Elsewhere: RCSB PDB 6U66 · PDBe 6U66 · UniProt Q15848
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