MolNFT v1 · #157667 · protein
Ftsy-ng high-resolution
6N6N · Signal recognition particle receptor ftsy: “Ftsy-ng high-resolution”. X-ray diffraction, 2 ligands (GCP, MG), 2 pockets (best druggability 0.82). MolNFT v1 #157667 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6N6N
- Type
- protein
- Length
- 602 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Signal recognition particle receptor ftsy
- UniProt
- P10121
- Ligands
- GCP, MG
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Signal recognition particle receptor ftsy | protein | 301 | 53% helix, 13% strand | P10121 |
Ligands and binding sites
- GCP · Phosphomethylphosphonic acid guanylate ester · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 5 copies · chains A, B
- ACT · Acetate ion · additive · chains A
- 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 | 773 | 0.82 | 0.85 | 62 | empty |
| 2 | 52 | 0.37 | 0.80 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 739 Ų buried · 13 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 6N6N · PDBe 6N6N · UniProt P10121
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