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Serum paraoxonase-1 by directed evolution with the K192Q mutation

Analyse Serum paraoxonase-1 by directed evolution with the K192Q mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4Q1U
Type: protein
Length: 328 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serum PARAOXONASE/ARYLESTERASE 1
EC: 3.1.1.2, 3.1.1.81, 3.1.8.1
Ligands: CA, PO4, CL, BR
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serum PARAOXONASE/ARYLESTERASE 1 (EC 3.1.1.2, 3.1.1.81, 3.1.8.1)	protein	328	9% helix, 48% strand	—

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A
PO4 · Phosphate ion · ion · chains A
CL · Chloride ion · ion · chains A
BR · Bromide ion · ion · chains A
LMT · Dodecyl-beta-D-maltoside · additive · chains A

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

Pockets

2 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	379	0.64	0.78	33	PO4
2	263	0.63	0.81	36	empty

Compared structures

4Q1U · Serum paraoxonase-1 by directed evolution with the K192Q mutation · 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
Elsewhere: RCSB PDB 4Q1U · PDBe 4Q1U

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