MolNFT v1 · #14027 · protein
Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain
1LVO: “Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra…”. X-ray diffraction. MolNFT v1 #14027 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1LVO
- Type
- protein
- Length
- 1,798 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9IW06
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E, F | — | protein | 299 | — | Q9IW06 |
| B, C | — | protein | 300 | — | Q9IW06 |
| D | — | protein | 301 | — | Q9IW06 |
Compared structures
- 1LVO · Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with… · 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 Q9IW06
- Elsewhere: RCSB PDB 1LVO · PDBe 1LVO · UniProt Q9IW06
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