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Alpha-esterase-7 in complex with [3-(benzyloxy)-4-METHYLPHENYL]BORINIC acid

Analyse Alpha-esterase-7 in complex with [3-(benzyloxy)-4-METHYLPHENYL]BORINIC acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TYO
Type: protein
Length: 566 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carboxylic ester hydrolase
EC: 3.1.1.-
UniProt: Q25252
Ligands: 7NM
Pockets: 3 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carboxylic ester hydrolase (EC 3.1.1.-)	protein	566	38% helix, 16% strand	Q25252

Ligands and binding sites

7NM · [3-(benzyloxy)-4-methylphenyl]borinic acid · ligand · chains A

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

Pockets

3 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	637	0.74	0.80	49	7NM
2	266	0.64	0.81	35	empty
3	158	0.57	0.82	31	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

5TYO · alpha-esterase-7 in complex with [3-(benzyloxy)-4-methylphenyl]borinic acid · 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 Q25252
Elsewhere: RCSB PDB 5TYO · PDBe 5TYO · UniProt Q25252

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