MolNFT v1 · #95323 · protein

Structural basis of substrate specificity and protease inhibition in norwalk virus

4IMQ · 3C-like protease: “Structural basis of substrate specificity and protease inhibition in norwalk virus”. X-ray diffraction, 3 ligands (PHQ, NA, SCN). MolNFT v1 #95323 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4IMQ
Type: protein
Length: 176 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3C-like protease; Peptide inhibitor, SYC8
EC: 3.4.22.66
UniProt: Q83883
Ligands: PHQ, NA, SCN

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3C-like protease (EC 3.4.22.66)	protein	173	8% helix, 50% strand	Q83883
B	Peptide inhibitor, SYC8	protein	3	0% helix, 0% strand	—

Ligands and binding sites

PHQ · benzyl chlorocarbonate · ligand · chains A, B
NA · Sodium ion · metal · chains A
SCN · Thiocyanate ion · ion · 2 copies · chains A

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

Interfaces

1 interface between chains.

A–B · 415 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

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

Compared structures

4IMQ · 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 4IMQ · PDBe 4IMQ · UniProt Q83883

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