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Structural basis of substrate specificity and protease inhibition in norwalk virus

Analyse Structural basis of substrate specificity and protease inhibition in norwalk… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4IN2
Type: protein
Length: 344 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: C-like protease
EC: 3.4.22.66
UniProt: Q83883
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	C-like protease (EC 3.4.22.66)	protein	173	6% helix, 49% strand	Q83883
B	C-like protease (EC 3.4.22.66)	protein	171	8% helix, 51% strand	Q83883

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	272	0.67	0.83	30	empty
2	65	0.33	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 454 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified, 2 disulfide (engineered, disulfide).

Compared structures

4IN2 · Structural Basis of Substrate Specificity and Protease Inhibition in Norwalk Virus · 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 Q83883
Elsewhere: RCSB PDB 4IN2 · PDBe 4IN2 · UniProt Q83883

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