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Esterase-6 from drosophila melanogaster

Analyse Esterase-6 from drosophila melanogaster in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5THM
Type: protein
Length: 520 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase-6
EC: 3.1.1.1
UniProt: P08171
Ligands: 7BZ
Pockets: 8 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Esterase-6 (EC 3.1.1.1)	protein	520	35% helix, 19% strand	P08171

Ligands and binding sites

7BZ · N,N-dimethylboranamine · ligand · chains A

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

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	262	0.77	0.90	31	7BZ
2	322	0.60	0.78	41	empty
3	125	0.41	0.75	19	empty
4	59	0.34	0.77	11	empty
5	57	0.31	0.76	16	empty

Modifications

Observed in the structure: 32 modified, 1 disulfide (methylation, disulfide).

Compared structures

5THM · Esterase-6 from Drosophila melanogaster · the same entry in another collection · chain A against A, TM-score 1.00
P08171 · AlphaFold monomer V2.0 prediction for esterase-6 (P08171) · 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 P08171
Elsewhere: RCSB PDB 5THM · PDBe 5THM · UniProt P08171

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