Research workbench

Escherichia COLI ffh in complex with pppgpp

Analyse Escherichia COLI ffh in complex with pppgpp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

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.

Pocket	Volume (Å³)	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

7O9I · Escherichia coli Ffh in complex with pppGpp · the same entry in another collection · chain A against A, TM-score 1.00
P0AGD7 · AlphaFold monomer V2.0 prediction for signal recognition particle protein (P0AGD7) · a predicted model of the same protein · chain A against A, TM-score 0.96

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

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.