Research workbench

Pre-cleavage structure of the autotransporter espp - N1023D mutant

Analyse Pre-cleavage structure of the autotransporter espp - N1023D mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3SLO
Type: protein
Length: 306 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serine protease espp
UniProt: Q7BSW5
Pockets: 4 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 68% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serine protease espp	protein	306	9% helix, 68% strand	Q7BSW5

Ligands and binding sites

C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 8 copies · chains A

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	185	0.81	0.96	41	empty
2	400	0.74	0.84	41	empty
3	161	0.56	0.81	26	empty
4	142	0.42	0.76	25	empty

Compared structures

3SLO · Pre-cleavage Structure of the Autotransporter EspP - N1023D mutant · the same entry in another collection · chain A against A, TM-score 1.00
Q7BSW5 · AlphaFold monomer V2.0 prediction for serine protease espp (Q7BSW5) · 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 Q7BSW5
Elsewhere: RCSB PDB 3SLO · PDBe 3SLO · UniProt Q7BSW5

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