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Deuterolysin from aspergillus oryzae

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

PDB: 1EB6
Type: protein
Length: 177 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neutral protease II
EC: 3.4.24.39
UniProt: P46076
Ligands: ZN
Pockets: 1 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Neutral protease II (EC 3.4.24.39)	protein	177	53% helix, 10% strand	P46076

Ligands and binding sites

ZN · Zinc ion · metal · chains A
EDO · 1,2-ethanediol · additive · 3 copies · 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	69	0.47	0.83	23	EDO

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1EB6 · Deuterolysin from Aspergillus oryzae · the same entry in another collection · chain A against A, TM-score 1.00
P46076 · AlphaFold monomer V2.0 prediction for neutral protease 2 (P46076) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P46076
Elsewhere: RCSB PDB 1EB6 · PDBe 1EB6 · UniProt P46076

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