Research workbench
Ftsy-ng high-resolution
Analyse Ftsy-ng high-resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6N5I
- Type
- protein
- Length
- 604 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Signal recognition particle receptor ftsy
- UniProt
- P10121
- Ligands
- K
- Pockets
- 6 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal recognition particle receptor ftsy | protein | 303 | 52% helix, 13% strand | P10121 |
| B | Signal recognition particle receptor ftsy | protein | 301 | 54% helix, 13% strand | P10121 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 643 | 0.82 | 0.87 | 56 | empty |
| 2 | 50 | 0.46 | 0.85 | 12 | K |
| 3 | 56 | 0.36 | 0.79 | 22 | empty |
| 4 | 81 | 0.36 | 0.76 | 16 | empty |
| 5 | 51 | 0.31 | 0.77 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 813 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
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 P10121
- Elsewhere: RCSB PDB 6N5I · PDBe 6N5I · UniProt P10121
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