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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: 4IMZ
Type: protein
Length: 176 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Genome polyprotein; Peptide inhibitor, syc 10
EC: 3.6.1.15, 3.4.22.66, 2.7.7.48
UniProt: Q83883
Ligands: PHQ, NA, SCN

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Genome polyprotein (EC 3.6.1.15, 3.4.22.66, 2.7.7.48)	protein	173	8% helix, 50% strand	Q83883
B	Peptide inhibitor, syc 10	protein	3	0% helix, 33% strand	—

Ligands and binding sites

PHQ · benzyl chlorocarbonate · ligand · chains A, B
NA · Sodium ion · metal · chains A
SCN · Thiocyanate ion · ion · 4 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

A–B · 454 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent, 1 modified (covalent ligand, nonstandard).

Compared structures

4IMZ · 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 4IMZ · PDBe 4IMZ · UniProt Q83883

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