Research workbench
Dual modes of modification of hepatitis a virus 3C protease by a serine derived beta-lactone: selective crytstallization and high resolution structure of the HIS102 adduct
Analyse Dual modes of modification of hepatitis a virus 3C protease by a serine derived… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A4O
- Type
- protein
- Length
- 214 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, ACE
- Pockets
- 2 · best druggability 0.48
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 | 214 | 18% helix, 49% strand | P13901 |
Ligands and binding sites
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.48 | 0.84 | 21 | empty |
| 2 | 124 | 0.43 | 0.76 | 24 | empty |
Modifications
Observed in the structure: 3 covalent, 1 modified (covalent ligand, nonstandard).
Compared structures
- 2A4O · 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 2A4O · PDBe 2A4O · UniProt P13901
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