Research workbench
Sjoegren syndrome/scleroderma autoantigen 1 (SSSCA1)
Analyse Sjoegren syndrome/scleroderma autoantigen 1 (SSSCA1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HCZ
- Type
- protein
- Length
- 130 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.3
- Source
- Homo sapiens
- Molecule
- Sjoegren syndrome/scleroderma autoantigen 1
- UniProt
- O60232
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · resolution 2.3 · 2 distinct chains · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sjoegren syndrome/scleroderma autoantigen 1 | protein | 65 | 40% helix, 18% strand | O60232 |
| B | Sjoegren syndrome/scleroderma autoantigen 1 | protein | 65 | 48% helix, 22% strand | O60232 |
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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 83 | 0.38 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1070 Ų buried · 12 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 O60232
- Elsewhere: RCSB PDB 6HCZ · PDBe 6HCZ · UniProt O60232
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