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Crystal structure of substrate-like, unprocessed N-terminal protease npro mutant S169P

Analyse Crystal structure of substrate-like, unprocessed N-terminal protease npro… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ZFO
Type: protein
Length: 150 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-terminal protease npro
EC: 3.4.22.-
UniProt: Q5L4B1
Ligands: CL, OH
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-terminal protease npro (EC 3.4.22.-)	protein	150	7% helix, 36% strand	Q5L4B1

Ligands and binding sites

CL · Chloride ion · ion · chains A
OH · Hydroxide ion · ion · chains A
SGM · Monothioglycerol · 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	89	0.34	0.74	19	empty

Modifications

Observed in the structure: 2 disulfide, 1 covalent (disulfide, additive adduct).

Compared structures

3ZFO · Crystal structure of substrate-like, unprocessed N-terminal protease Npro mutant S169P · 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 Q5L4B1
Elsewhere: RCSB PDB 3ZFO · PDBe 3ZFO · UniProt Q5L4B1

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