Research workbench
N and GTPase domains of the signal sequence recognition protein ffh from thermus aquaticus
Analyse N and GTPase domains of the signal sequence recognition protein ffh from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NG1
- Type
- protein
- Length
- 293 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Signal sequence recognition protein ffh
- UniProt
- O07347
- Ligands
- GDP
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal sequence recognition protein ffh | protein | 293 | 54% helix, 14% strand | O07347 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
- DIO · 1,4-diethylene dioxide · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 82 | 0.67 | 0.92 | 23 | EDO |
| 2 | 78 | 0.42 | 0.79 | 15 | DIO |
| 3 | 63 | 0.42 | 0.82 | 21 | empty |
| 4 | 67 | 0.34 | 0.77 | 12 | empty |
Compared structures
- 2NG1 · N and GTPase domains of the signal sequence recognition protein ffh from thermus aquaticus · the same entry in another collection · chain A against A, TM-score 1.00
- O07347 · AlphaFold monomer V2.0 prediction for signal recognition particle protein (O07347) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O07347
- Elsewhere: RCSB PDB 2NG1 · PDBe 2NG1 · UniProt O07347
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