Research workbench
Monoclinic crystal structure of salmonella flga in closed form
Analyse Monoclinic crystal structure of salmonella flga in closed form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VKI
- Type
- protein
- Length
- 792 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagella basal body P-ring formation protein flga
- UniProt
- P40131
- Pockets
- 9 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Flagella basal body P-ring formation protein flga | protein | 198 | 12% helix, 44% strand | P40131 |
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 | 658 | 0.60 | 0.73 | 100 | empty |
| 2 | 182 | 0.57 | 0.81 | 40 | empty |
| 3 | 159 | 0.52 | 0.79 | 34 | empty |
| 4 | 213 | 0.46 | 0.73 | 33 | empty |
| 5 | 167 | 0.44 | 0.75 | 32 | empty |
Interfaces
6 interfaces between chains.
- A–D · 696 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 683 Ų buried · 21 hydrogen bonds · protein-protein
- B–C · 668 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 627 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 284 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3VKI · Monoclinic Crystal Structure of Salmonella FlgA in closed form · the same entry in another collection · chain D against D, TM-score 1.00
- P40131 · AlphaFold monomer V2.0 prediction for flagella basal body P-ring formation protein flga… · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P40131
- Elsewhere: RCSB PDB 3VKI · PDBe 3VKI · UniProt P40131
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