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The molecular mechanism of enantiorecognition by esterases

Analyse The molecular mechanism of enantiorecognition by esterases in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ESE
Type: protein
Length: 302 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase
UniProt: P22266
Ligands: DEP
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Esterase	protein	302	41% helix, 13% strand	P22266

Ligands and binding sites

DEP · Diethyl phosphonate · ligand · chains A

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

Pockets

2 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	228	0.69	0.85	42	DEP
2	57	0.30	0.75	12	empty

Modifications

Observed in the structure: 3 disulfide, 1 covalent (disulfide, covalent ligand).

Compared structures

1ESE · The molecular mechanism of enantiorecognition by esterases · the same entry in another collection · chain A against A, TM-score 1.00
P22266 · AlphaFold monomer V2.0 prediction for esterase (P22266) · a predicted model of the same protein · 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 P22266
Elsewhere: RCSB PDB 1ESE · PDBe 1ESE · UniProt P22266

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