Research workbench
Crystal structure of unbound SARS coronavirus main peptidase in the space group C2
Analyse Crystal structure of unbound SARS coronavirus main peptidase in the space group… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A5A
- Type
- protein
- Length
- 306 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3C-like peptidase
- EC
- 3.4.22.-
- UniProt
- P59641
- Ligands
- CL
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3C-like peptidase (EC 3.4.22.-) | protein | 306 | 24% helix, 28% strand | P59641 |
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 | 180 | 0.45 | 0.75 | 25 | CL |
| 2 | 130 | 0.42 | 0.75 | 24 | empty |
Compared structures
- 2A5A · Crystal structure of unbound SARS coronavirus main peptidase in the space group C2 · 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 P59641
- Elsewhere: RCSB PDB 2A5A · PDBe 2A5A · UniProt P59641
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