MolNFT v1 · #33878 · protein

Dual modes of modification of hepatitis a virus 3C protease by a serine-derived betalactone: selective crystallization and high- resolution structure of the his-102 adduct

2CXV · Probable protein P3C: “Dual modes of modification of hepatitis a virus 3C protease by a serine-derived betalactone: selective…”. X-ray diffraction, 1 ligand (BBL), 2 pockets (best druggability 0.49). MolNFT v1 #33878 on GenesisL1…

PDB: 2CXV
Type: protein
Length: 212 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Probable protein P3C
EC: 3.4.22.28
UniProt: P13901
Ligands: BBL
Pockets: 2 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Probable protein P3C (EC 3.4.22.28)	protein	212	18% helix, 49% strand	P13901

Ligands and binding sites

BBL · N-[(benzyloxy)carbonyl]-L-alanine · 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	178	0.49	0.77	27	empty
2	52	0.29	0.75	18	empty

Modifications

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

Compared structures

2CXV · Dual Modes of Modification of Hepatitis A Virus 3C Protease by a Serine-Derived… · 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 P13901
Elsewhere: RCSB PDB 2CXV · PDBe 2CXV · UniProt P13901

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