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
- 6NC4
- Type
- protein
- Length
- 606 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Signal recognition particle receptor ftsy
- UniProt
- P10121
- Ligands
- GNP, GDP, NH4
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Signal recognition particle receptor ftsy | protein | 303 | 51% helix, 14% strand | P10121 |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
- GDP · Guanosine-5'-diphosphate · ligand · chains B
- NH4 · Ammonium ion · ion · 20 copies · chains A, B
- ACT · Acetate ion · additive · 8 copies · chains A, B
- GOL · Glycerol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 710 | 0.82 | 0.86 | 64 | NH4, ACT |
| 2 | 93 | 0.39 | 0.76 | 15 | ACT |
Interfaces
1 interface between chains.
- A–B · 871 Ų buried · 16 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 6NC4 · PDBe 6NC4 · UniProt P10121
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