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: 6N5J
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: NH4
Pockets: 3 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Signal recognition particle receptor ftsy	protein	301	54% helix, 13% strand	P10121

Ligands and binding sites

NH4 · Ammonium ion · ion · 2 copies · chains A
ACT · Acetate ion · additive · chains B

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	637	0.81	0.86	52	empty
2	141	0.40	0.74	32	empty
3	73	0.37	0.77	17	empty

Interfaces

1 interface between chains.

A–B · 727 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

6N5J · FtsY-NG high-resolution · the same entry in another collection · chain A against A, TM-score 1.00
P10121 · AlphaFold monomer V2.0 prediction for signal recognition particle receptor ftsy (P10121) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 6N5J · PDBe 6N5J · UniProt P10121

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