MolNFT v1 · #135422 · protein

Alpha-esterase-7 in complex with [3-bromo-5-(pyrrolidin-1-yl) PHENYL]BORINIC acid

5TYM · Carboxylic ester hydrolase: “Alpha-esterase-7 in complex with [3-bromo-5-(pyrrolidin-1-yl) PHENYL]BORINIC acid”. X-ray diffraction, 1 ligand (7NS), 4 pockets (best druggability 0.73). MolNFT v1 #135422 on GenesisL1: 3D structure…

PDB: 5TYM
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: 7NS
Pockets: 4 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carboxylic ester hydrolase (EC 3.1.1.-)	protein	566	38% helix, 17% strand	Q25252

Ligands and binding sites

7NS · [3-bromo-5-(pyrrolidin-1-yl)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	662	0.73	0.79	49	7NS
2	250	0.65	0.82	37	empty
3	169	0.58	0.82	33	empty
4	50	0.24	0.72	13	empty

Modifications

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

Compared structures

5TYM · alpha-esterase-7 in complex with [3-bromo-5-(pyrrolidin-1-yl)phenyl]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 5TYM · PDBe 5TYM · UniProt Q25252

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