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Crystal structure of twin-arginine translocation pathway signal protein from burkholderia phytofirmans

Analyse Crystal structure of twin-arginine translocation pathway signal protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2RJO
Type: protein
Length: 322 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Twin-arginine translocation pathway signal protein
UniProt: A0GG20
Ligands: GAL, SO4
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Twin-arginine translocation pathway signal protein	protein	322	46% helix, 21% strand	A0GG20

Ligands and binding sites

GAL · beta-D-galactopyranose · sugar · chains A
SO4 · Sulfate ion · ion · 4 copies · 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	88	0.59	0.88	25	GAL, SO4
2	112	0.47	0.79	25	SO4
3	89	0.43	0.79	19	SO4

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

2RJO · Crystal structure of Twin-arginine translocation pathway signal protein from Burkholderia… · 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 A0GG20
Elsewhere: RCSB PDB 2RJO · PDBe 2RJO · UniProt A0GG20

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