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C-terminal LG domain pair of human Gas6
Analyse C-terminal LG domain pair of human Gas6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H30
- Type
- protein
- Length
- 391 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.2
- Source
- HOMO SAPIENS
- Molecule
- Growth-arrest-specific protein
- UniProt
- Q14393
- Ligands
- CA, SO4
- Pockets
- 6 · best druggability 0.61
Structure
x-ray diffraction · resolution 2.2 · 1 distinct chain · 8% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Growth-arrest-specific protein | protein | 391 | 8% helix, 47% strand | Q14393 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 255 | 0.61 | 0.80 | 32 | empty |
| 2 | 155 | 0.56 | 0.82 | 30 | empty |
| 3 | 88 | 0.42 | 0.78 | 19 | empty |
| 4 | 89 | 0.38 | 0.76 | 26 | empty |
| 5 | 52 | 0.33 | 0.78 | 15 | empty |
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 Q14393
- Elsewhere: RCSB PDB 1H30 · PDBe 1H30 · UniProt Q14393
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