MolNFT v1 · #120608 · protein
Crystal structure of the flagellar cap protein flid D2-D3 domains from salmonella typhimurium
5H5T · Flagellar hook-associated protein 2: “Crystal structure of the flagellar cap protein flid D2-D3 domains from salmonella typhimurium”. X-ray diffraction, 6 pockets (best druggability 0.58). MolNFT v1 #120608 on GenesisL1: 3D…
- PDB
- 5H5T
- Type
- protein
- Length
- 976 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar hook-associated protein 2
- UniProt
- A0A0D6FM27
- Pockets
- 6 · best druggability 0.58
Structure
x-ray diffraction · 3 distinct chains · 11% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E | Flagellar hook-associated protein 2 | protein | 196 | 10% helix, 51% strand | A0A0D6FM27 |
| B | Flagellar hook-associated protein 2 | protein | 195 | 11% helix, 51% strand | A0A0D6FM27 |
| D | Flagellar hook-associated protein 2 | protein | 193 | 11% helix, 47% strand | A0A0D6FM27 |
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 332 | 0.58 | 0.77 | 47 | empty |
| 2 | 298 | 0.55 | 0.76 | 41 | empty |
| 3 | 279 | 0.55 | 0.77 | 47 | empty |
| 4 | 288 | 0.52 | 0.75 | 50 | empty |
| 5 | 164 | 0.45 | 0.75 | 29 | empty |
Interfaces
5 interfaces between chains.
- B–C · 689 Ų buried · 6 hydrogen bonds · protein-protein
- A–E · 651 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 647 Ų buried · 8 hydrogen bonds · protein-protein
- D–E · 625 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 590 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 5H5T · Crystal structure of the flagellar cap protein FliD D2-D3 domains from Salmonella… · 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 A0A0D6FM27
- Elsewhere: RCSB PDB 5H5T · PDBe 5H5T · UniProt A0A0D6FM27
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