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The salmonella virulence effector SSPH2 functions as a novel E3 ligase

Analyse The salmonella virulence effector SSPH2 functions as a novel E3 ligase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3G06
Type: protein
Length: 601 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SSPH2 (leucine-rich repeat protein)
EC: 6.3.2.19
UniProt: Q9RPH0
Pockets: 1 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SSPH2 (leucine-rich repeat protein) (EC 6.3.2.19)	protein	601	42% helix, 8% strand	Q9RPH0

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	65	0.39	0.79	20	empty

Compared structures

3G06 · The Salmonella Virulence Effector SspH2 Functions As A Novel E3 Ligase · 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 Q9RPH0
Elsewhere: RCSB PDB 3G06 · PDBe 3G06 · UniProt Q9RPH0

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