MolNFT v1 · #135420 · protein

Alpha-esterase-7 in complex with 3-chloro-4-[(2-fluorophenyl) METHOXY]PHENYLBORINIC acid

5TYK · Carboxylic ester hydrolase: “Alpha-esterase-7 in complex with 3-chloro-4-[(2-fluorophenyl) METHOXY]PHENYLBORINIC acid”. X-ray diffraction, 1 ligand (7N4), 4 pockets (best druggability 0.76). MolNFT v1 #135420 on GenesisL1: 3D…

PDB: 5TYK
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: 7N4
Pockets: 4 · best druggability 0.76

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

7N4 · {3-chloro-4-[(2-fluorophenyl)methoxy]phenyl}borinic acid · ligand · 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	753	0.76	0.80	58	7N4
2	200	0.59	0.81	39	empty
3	178	0.57	0.81	31	empty
4	52	0.31	0.76	10	empty

Modifications

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

Compared structures

5TYK · alpha-esterase-7 in complex with 3-chloro-4-[(2-fluorophenyl)methoxy]phenylborinic 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 5TYK · PDBe 5TYK · UniProt Q25252

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