Research workbench
Shewanella frigidimarina ice-binding PROTEIN_1 DUF3494 domain
Analyse Shewanella frigidimarina ice-binding PROTEIN_1 DUF3494 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BG8
- Type
- protein
- Length
- 478 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ig domain protein, group 2 domain protein
- UniProt
- Q086E4
- Ligands
- SO4, CL, PO4
- Pockets
- 2 · best druggability 0.27
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ig domain protein, group 2 domain protein | protein | 239 | 13% helix, 38% strand | Q086E4 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · 4 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 | 55 | 0.27 | 0.74 | 13 | empty |
| 2 | 51 | 0.25 | 0.73 | 13 | empty |
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 Q086E4
- Elsewhere: RCSB PDB 6BG8 · PDBe 6BG8 · UniProt Q086E4
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