2CXV
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
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A | Probable protein P3C | polymer | 219 | 24119.8 | 1 | UniProt (P13901) Pfam (PF00548) In PDB | Human hepatitis A virus Hu/Northern Africa/MBB/1978 | 3C protease |
2 | A | N-[(BENZYLOXY)CARBONYL]-L-ALANINE | non-polymer | 223.2 | 1 | Chemie (BBL) | |||
3 | water | water | 18.0 | 247 | Chemie (HOH) |
Sequence modifications
A: 1 - 219 (UniProt: P13901)
PDB | External Database | Details |
---|---|---|
Ser 24 | Cys 1543 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 1 |
Total formula weight | 24119.8 | |
Non-Polymers* | Number of molecules | 1 |
Total formula weight | 223.2 | |
All* | Total formula weight | 24343.0 |