MolNFT v1 · #134738 · protein
Structure of cofolded FLIFC:FLIGN complex from thermotoga maritima
5TDY · Flagellar M-ring protein: “Structure of cofolded FLIFC:FLIGN complex from thermotoga maritima”. X-ray diffraction, 2 pockets (best druggability 0.49). MolNFT v1 #134738 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5TDY
- Type
- protein
- Length
- 260 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar M-ring protein; Flagellar motor switch protein flig
- UniProt
- Q9WY64, Q9WY63
- Pockets
- 2 · best druggability 0.49
Structure
x-ray diffraction · 4 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flagellar M-ring protein | protein | 35 | 89% helix, 0% strand | Q9WY64 |
| B | Flagellar motor switch protein flig | protein | 95 | 72% helix, 0% strand | Q9WY63 |
| C | Flagellar M-ring protein | protein | 42 | 79% helix, 0% strand | Q9WY64 |
| D | Flagellar motor switch protein flig | protein | 88 | 77% helix, 0% strand | Q9WY63 |
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 | 247 | 0.49 | 0.74 | 29 | empty |
| 2 | 107 | 0.36 | 0.73 | 12 | empty |
Interfaces
4 interfaces between chains.
- C–D · 1523 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 1322 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 83 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 39 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 5TDY · Structure of cofolded FliFc:FliGn complex from Thermotoga maritima · the same entry in another collection · chain A against A, TM-score 1.00
- Q9WY63 · AlphaFold monomer V2.0 prediction for flagellar motor switch protein flig (Q9WY63) · a predicted model of the same protein · chain D against A, TM-score 0.82
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 Q9WY64
- Every structure of UniProt Q9WY63
- Elsewhere: RCSB PDB 5TDY · PDBe 5TDY · UniProt Q9WY64 · UniProt Q9WY63
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