Research workbench
The crystal structure of a complment-1Q family protein suggests an evolutionary link to tumor necrosis factor
Analyse The crystal structure of a complment-1Q family protein suggests an evolutionary… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1C28
- Type
- protein
- Length
- 338 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Mus musculus
- Molecule
- Protein (30 kd adipocyte complement-related protein precursor (ACRP30))
- UniProt
- Q60994
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · resolution 2.1 · 3 distinct chains · 0% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (30 kd adipocyte complement-related protein precursor (ACRP30)) | protein | 125 | 0% helix, 56% strand | Q60994 |
| B | Protein (30 kd adipocyte complement-related protein precursor (ACRP30)) | protein | 111 | 0% helix, 54% strand | Q60994 |
| C | Protein (30 kd adipocyte complement-related protein precursor (ACRP30)) | protein | 102 | 0% helix, 53% strand | Q60994 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 260 | 0.77 | 0.90 | 37 | empty |
| 2 | 163 | 0.52 | 0.79 | 30 | empty |
| 3 | 186 | 0.47 | 0.75 | 20 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1221 Ų buried · 23 hydrogen bonds · protein-protein
- A–C · 824 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 681 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 1C28 · The crystal structure of a complment-1Q family protein suggests an evolutionary link to… · the same entry in another collection · chain A against A, TM-score 1.00
- Q60994 · AlphaFold monomer V2.0 prediction for adiponectin (Q60994) · a predicted model of the same protein · chain C against A, TM-score 0.94
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 Q60994
- Elsewhere: RCSB PDB 1C28 · PDBe 1C28 · UniProt Q60994
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