Research workbench
Averaged strand structure of a 15-stranded parm filament from clostridium botulinum
Analyse Averaged strand structure of a 15-stranded parm filament from clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IZV
- Type
- protein
- Length
- 698 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative plasmid segregation protein parm
- UniProt
- A0A0B4W229
- Ligands
- ADP, MG
- Pockets
- 9 · best druggability 0.71
Structure
electron microscopy · 1 distinct chain · 33% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 0, 1 | Putative plasmid segregation protein parm | protein | 349 | 33% helix, 25% strand | A0A0B4W229 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains 0, 1
- MG · Magnesium ion · metal · 2 copies · chains 0, 1
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 447 | 0.71 | 0.82 | 50 | ADP, MG |
| 2 | 393 | 0.71 | 0.82 | 52 | ADP, MG |
| 3 | 111 | 0.55 | 0.84 | 26 | empty |
| 4 | 128 | 0.49 | 0.79 | 18 | empty |
| 5 | 75 | 0.47 | 0.83 | 20 | empty |
Interfaces
1 interface between chains.
- 0–1 · 1214 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 6IZV · Averaged strand structure of a 15-stranded ParM filament from Clostridium botulinum · the same entry in another collection · chain 0 against 0, 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 A0A0B4W229
- Elsewhere: RCSB PDB 6IZV · PDBe 6IZV · UniProt A0A0B4W229
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