MolNFT v1 · #118371 · protein

Venezuelan equine encephalitis virus (veev) nonstructural protein 2 (NSP2) cysteine protease inhibited by E64D

5EZS · Non-structural protein 2 cysteine protease: “Venezuelan equine encephalitis virus (veev) nonstructural protein 2 (NSP2) cysteine protease inhibited by E64D”. X-ray diffraction, 1 ligand (E6D), 2 pockets (best druggability 0.41).…

PDB: 5EZS
Type: protein
Length: 320 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Non-structural protein 2 cysteine protease
EC: 3.4.22.-
UniProt: P27282
Ligands: E6D
Pockets: 2 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Non-structural protein 2 cysteine protease (EC 3.4.22.-)	protein	320	33% helix, 20% strand	P27282

Ligands and binding sites

E6D · ethyl (3S)-3-hydroxy-4-({(2S)-4-methyl-1-[(3-methylbutyl)amino]-1-oxopentan-2-yl}amino)-4-oxobutanoate · ligand · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	103	0.41	0.77	24	empty
2	116	0.38	0.74	22	E6D

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

5EZS · Venezuelan Equine Encephalitis Virus (VEEV) Nonstructural Protein 2 (nsP2) Cysteine… · 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 P27282
Elsewhere: RCSB PDB 5EZS · PDBe 5EZS · UniProt P27282

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.