Research workbench
Structure of the SARS-cov-2 3CL protease in complex with inhibitor 18
Analyse Structure of the SARS-cov-2 3CL protease in complex with inhibitor 18 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7M2P
- Type
- protein
- Length
- 309 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DTD1
- Ligands
- P6S
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 306 | — | P0DTD1 |
| B | — | protein | 3 | — | — |
Ligands and binding sites
- P6S · benzyl hydrogen carbonate · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7M2P · Structure of the SARS-CoV-2 3CL protease in complex with inhibitor 18 · 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 P0DTD1
- Elsewhere: RCSB PDB 7M2P · PDBe 7M2P · UniProt P0DTD1
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