Research workbench

Crystal structure of E6H variant of de novo designed serine hydrolase OSH55, northeast structural genomics consortium (nesg) target OR185

Analyse Crystal structure of E6H variant of de novo designed serine hydrolase OSH55… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ETJ
Type: protein
Length: 164 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serine hydrolase
Ligands: PE6, CL
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serine hydrolase	protein	164	38% helix, 22% strand	—

Ligands and binding sites

PE6 · Phosphoryl-hexaethylene glycol · ligand · chains A
CL · Chloride ion · ion · chains A
PE4 · 2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-ethanol · additive · chains A
PE5 · 3,6,9,12,15,18,21,24-octaoxahexacosan-1-ol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	209	0.59	0.80	40	PE5, PE6

Compared structures

4ETJ · Crystal Structure of E6H variant of de novo designed serine hydrolase OSH55, Northeast… · 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
Elsewhere: RCSB PDB 4ETJ · PDBe 4ETJ

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