Research workbench
X-ray structure of bacteriocin as-48 at pH 4.5. sulphate bound form
Analyse X-ray structure of bacteriocin as-48 at pH 4.5. sulphate bound form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1O82
- Type
- protein
- Length
- 280 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptide antibiotic as-48
- UniProt
- Q47765
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Peptide antibiotic as-48 | protein | 70 | 77% helix, 0% strand | Q47765 |
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 | 134 | 0.53 | 0.81 | 23 | GOL, SO4 |
Interfaces
3 interfaces between chains.
- B–D · 505 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 428 Ų buried · 1 hydrogen bond · protein-protein
- C–D · 415 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1O82 · X-ray structure of bacteriocin as-48 at pH 4.5. sulphate bound form · the same entry in another collection · chain A against A, TM-score 1.00
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 Q47765
- Elsewhere: RCSB PDB 1O82 · PDBe 1O82 · UniProt Q47765
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