MolNFT v1 · #183983 · protein
Escherichia COLI ffh in complex with pppgpp
7O9I · Signal recognition particle protein: “Escherichia COLI ffh in complex with pppgpp”. X-ray diffraction, 1 ligand (C1Z), 3 pockets (best druggability 0.65). MolNFT v1 #183983 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 7O9I
- Type
- protein
- Length
- 286 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Signal recognition particle protein
- UniProt
- P0AGD7
- Ligands
- C1Z
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal recognition particle protein | protein | 286 | 52% helix, 13% strand | P0AGD7 |
Ligands and binding sites
- C1Z · Guanosine 3'-diphosphate 5'-triphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 194 | 0.65 | 0.84 | 34 | empty |
| 2 | 106 | 0.45 | 0.79 | 25 | C1Z |
| 3 | 65 | 0.41 | 0.80 | 15 | empty |
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 P0AGD7
- Elsewhere: RCSB PDB 7O9I · PDBe 7O9I · UniProt P0AGD7
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