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Crystal structure of SMG1 F278N mutant

Analyse Crystal structure of SMG1 F278N mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ZRD
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, BMA
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	LIP1, secretory lipase (family 3)	protein	278	31% 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 · 2 copies · chains A
BMA · beta-D-mannopyranose · sugar
GOL · Glycerol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	70	0.42	0.80	18	GOL

Modifications

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

Compared structures

4ZRD · Crystal structure of SMG1 F278N 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 A8PUY1
Elsewhere: RCSB PDB 4ZRD · PDBe 4ZRD · UniProt A8PUY1

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