Research workbench
Alfa from B. subtilis plasmid PLS32 filament structure at 3.4 a
Analyse Alfa from B. subtilis plasmid PLS32 filament structure at 3.4 a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F95
- Type
- protein
- Length
- 1,335 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alfa
- UniProt
- O52947
- Ligands
- ADP, MG
- Pockets
- 16 · best druggability 0.75
Structure
electron microscopy · 1 distinct chain · 22% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Alfa | protein | 267 | 22% helix, 30% strand | O52947 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains A, B, C, D, E
- MG · Magnesium ion · metal · 5 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 658 | 0.75 | 0.81 | 83 | MG, ADP |
| 2 | 583 | 0.73 | 0.81 | 67 | empty |
| 3 | 572 | 0.72 | 0.80 | 65 | empty |
| 4 | 127 | 0.59 | 0.85 | 25 | MG, ADP |
| 5 | 136 | 0.59 | 0.84 | 24 | MG, ADP |
Interfaces
7 interfaces between chains.
- A–C · 618 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 614 Ų buried · 6 hydrogen bonds · protein-protein
- B–E · 594 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 589 Ų buried · 3 hydrogen bonds · protein-protein
- A–E · 586 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6F95 · AlfA from B. subtilis plasmid pLS32 filament structure at 3.4 A · 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 O52947
- Elsewhere: RCSB PDB 6F95 · PDBe 6F95 · UniProt O52947
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