Research workbench

E.COLI thioesterase I/PROTEASE I/LYSOPHOSPHOLIASE L1

Analyse E.COLI thioesterase I/PROTEASE I/LYSOPHOSPHOLIASE L1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IVN
Type: protein
Length: 178 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioesterase I
EC: 3.1.1.5, 3.1.2.-
UniProt: P29679
Ligands: SO4
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioesterase I (EC 3.1.1.5, 3.1.2.-)	protein	178	51% helix, 15% strand	P29679

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	104	0.48	0.80	20	GOL

Compared structures

1IVN · E.coli Thioesterase I/Protease I/Lysophospholiase L1 · 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 P29679
Elsewhere: RCSB PDB 1IVN · PDBe 1IVN · UniProt P29679

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