Research workbench

Crystal structure of mono- and diacylglycerol lipase from malassezia globosa

Analyse Crystal structure of mono- and diacylglycerol lipase from malassezia globosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3UUF
Type: protein
Length: 278 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: LIP1, secretory lipase (family 3)
UniProt: A8PUY1
Ligands: NAG, MAN
Pockets: 2 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	LIP1, secretory lipase (family 3)	protein	278	32% helix, 23% strand	A8PUY1

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
MAN · alpha-D-mannopyranose · sugar · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	53	0.43	0.83	18	empty
2	53	0.42	0.83	14	empty

Modifications

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

Compared structures

3UUF · Crystal structure of mono- and diacylglycerol lipase from Malassezia globosa · 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 A8PUY1
Elsewhere: RCSB PDB 3UUF · PDBe 3UUF · UniProt A8PUY1

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.