Research workbench
PHUZ201 filament
Analyse PHUZ201 filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3J5V
- Type
- protein
- Length
- 311 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PHUZ201 subunit
- UniProt
- B3FK34
- Ligands
- GDP, MG
- Pockets
- 2 · best druggability 0.45
Structure
electron microscopy · 1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| a | PHUZ201 subunit | protein | 311 | 42% helix, 20% strand | B3FK34 |
Ligands and binding sites
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 | 144 | 0.45 | 0.77 | 30 | GDP, MG |
| 2 | 62 | 0.29 | 0.74 | 16 | empty |
Compared structures
- 3J5V · PhuZ201 filament · 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 B3FK34
- Elsewhere: RCSB PDB 3J5V · PDBe 3J5V · UniProt B3FK34
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