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Crystal structure analysis of the G84S EST2 mutant

Analyse Crystal structure analysis of the G84S EST2 mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2HM7
Type: protein
Length: 308 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carboxylesterase
EC: 3.1.1.1
UniProt: Q7SIG1
Ligands: SO4
Pockets: 3 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carboxylesterase (EC 3.1.1.1)	protein	308	40% helix, 20% strand	Q7SIG1

Ligands and binding sites

SO4 · Sulfate ion · ion · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	108	0.44	0.78	23	empty
2	115	0.41	0.76	19	SO4
3	52	0.31	0.76	16	empty

Compared structures

2HM7 · Crystal Structure Analysis of the G84S EST2 mutant · 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 2HM7 · PDBe 2HM7 · UniProt Q7SIG1

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