Research workbench

Escherichia COLI ftsy in complex with pppgpp

Analyse Escherichia COLI ftsy 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: 7O9H
Type: protein
Length: 605 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Signal recognition particle receptor ftsy
UniProt: A0A7D5IKJ2
Ligands: C1Z
Pockets: 5 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 54% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Signal recognition particle receptor ftsy	protein	302	53% helix, 14% strand	A0A7D5IKJ2
B	Signal recognition particle receptor ftsy	protein	303	54% helix, 13% strand	A0A7D5IKJ2

Ligands and binding sites

C1Z · Guanosine 3'-diphosphate 5'-triphosphate · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 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	787	0.77	0.81	57	empty
2	89	0.41	0.78	24	C1Z
3	60	0.40	0.81	19	empty
4	71	0.34	0.76	17	empty
5	59	0.29	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 744 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

7O9H · Escherichia coli FtsY in complex with pppGpp · the same entry in another collection · chain A against A, TM-score 1.00

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 A0A7D5IKJ2
Elsewhere: RCSB PDB 7O9H · PDBe 7O9H · UniProt A0A7D5IKJ2

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