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Crystal structure of aspergillus oryzae aspartic proteinase

Analyse Crystal structure of aspergillus oryzae aspartic proteinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IZD
Type: protein
Length: 323 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aspartic proteinase
UniProt: Q9URD0
Ligands: MAN
Pockets: 1 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aspartic proteinase	protein	323	12% helix, 48% strand	Q9URD0

Ligands and binding sites

MAN · alpha-D-mannopyranose · sugar · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	287	0.54	0.75	37	empty

Modifications

Observed in the structure: 1 glycan (O-glycosylation).

Compared structures

1IZD · Crystal structure of Aspergillus oryzae Aspartic Proteinase · 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 Q9URD0
Elsewhere: RCSB PDB 1IZD · PDBe 1IZD · UniProt Q9URD0

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