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Comparison of the structure and activity of glycosylated and aglycosylated human carboxylesterase 1

Analyse Comparison of the structure and activity of glycosylated and aglycosylated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5A7F
Type: protein
Length: 532 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Liver carboxylesterase 1
EC: 3.1.1.1, 3.1.1.56
Ligands: NAG, PO4
Pockets: 7 · best druggability 0.80

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Liver carboxylesterase 1 (EC 3.1.1.1, 3.1.1.56)	protein	532	38% helix, 17% strand	—

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
PO4 · Phosphate ion · ion · 2 copies · chains A

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

Pockets

7 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	133	0.80	0.97	27	empty
2	330	0.63	0.79	43	empty
3	72	0.41	0.80	16	empty
4	89	0.39	0.77	21	empty
5	92	0.34	0.74	18	empty

Modifications

Observed in the structure: 2 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

5A7F · Comparison of the structure and activity of glycosylated and aglycosylated Human… · 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 5A7F · PDBe 5A7F

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