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The three-dimensional structure of pngase F, a glycosylasparaginase from flavobacterium meningosepticum

Analyse The three-dimensional structure of pngase F, a glycosylasparaginase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PGS
Type: protein
Length: 311 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptide-N(4)-(N-acetyl-beta-D-glucosaminyl) asparagine amidase F
EC: 3.5.1.52
UniProt: P21163
Pockets: 1 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptide-N(4)-(N-acetyl-beta-D-glucosaminyl) asparagine amidase F (EC 3.5.1.52)	protein	311	5% helix, 47% strand	P21163

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	84	0.47	0.81	20	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1PGS · The three-dimensional structure of pngase F, a glycosylasparaginase from flavobacterium… · the same entry in another collection · chain A against A, TM-score 1.00
P21163 · AlphaFold monomer V2.0 prediction for peptide-N(4)-(N-acetyl-beta-D… · a predicted model of the same protein · 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 P21163
Elsewhere: RCSB PDB 1PGS · PDBe 1PGS · UniProt P21163

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