Research workbench
Structure of putative flagellar hook-associated protein from vibrio parahaemolyticus
Analyse Structure of putative flagellar hook-associated protein from vibrio… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PWX
- Type
- protein
- Length
- 418 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative flagellar hook-associated protein
- UniProt
- Q87JH9
- Ligands
- MG
- Pockets
- 5 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 68% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative flagellar hook-associated protein | protein | 224 | 65% helix, 7% strand | Q87JH9 |
| B | Putative flagellar hook-associated protein | protein | 194 | 72% helix, 6% strand | Q87JH9 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.52 | 0.87 | 12 | empty |
| 2 | 197 | 0.51 | 0.77 | 23 | empty |
| 3 | 198 | 0.49 | 0.76 | 20 | empty |
| 4 | 72 | 0.31 | 0.74 | 16 | empty |
| 5 | 62 | 0.30 | 0.74 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 620 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 3PWX · Structure of putative flagellar hook-associated protein from Vibrio parahaemolyticus · 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 Q87JH9
- Elsewhere: RCSB PDB 3PWX · PDBe 3PWX · UniProt Q87JH9
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