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Crystal structure of mutant M211S/R215L of carboxylesterase EST2 complexed with hexadecanesulfonate

Analyse Crystal structure of mutant M211S/R215L of carboxylesterase EST2 complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QZ3
Type: protein
Length: 309 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carboxylesterase EST2
UniProt: Q7SIG1
Ligands: HDS
Pockets: 3 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carboxylesterase EST2	protein	309	40% helix, 19% strand	Q7SIG1

Ligands and binding sites

HDS · 1-hexadecanosulfonic 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	304	0.73	0.85	39	HDS
2	129	0.62	0.86	24	empty
3	73	0.34	0.76	20	empty

Modifications

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

Compared structures

1QZ3 · Crystal structure of mutant M211S/R215L of carboxylesterase EST2 complexed with… · 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 Q7SIG1
Elsewhere: RCSB PDB 1QZ3 · PDBe 1QZ3 · UniProt Q7SIG1

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