Research workbench
Crystal structure of the SARS-cov-2 main protease in complex with Y180
Analyse Crystal structure of the SARS-cov-2 main protease in complex with Y180 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7FAZ
- Type
- protein
- Length
- 606 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DTC1
- Ligands
- 2RI, NA
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 301 | — | P0DTC1 |
| B | — | protein | 305 | — | P0DTC1 |
Ligands and binding sites
- 2RI · (2~{R})-~{N}-dibenzofuran-3-yl-~{N}-[(1~{R})-2-[[(1~{S})-1-(4-fluorophenyl)ethyl]amino]-2-oxidanylidene-1-pyridin-3-yl-ethyl]-2-oxidanyl-propanamide · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7FAZ · Crystal structure of the SARS-CoV-2 main protease in complex with Y180 · 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 P0DTC1
- Elsewhere: RCSB PDB 7FAZ · PDBe 7FAZ · UniProt P0DTC1
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