Research workbench
Complex structure of SARS-cov 3CL protease with tg-0204998
Analyse Complex structure of SARS-cov 3CL protease with tg-0204998 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZU4
- Type
- protein
- Length
- 306 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3C-like proteinase
- EC
- 3.4.22.-
- UniProt
- P0C6U8
- Ligands
- ZU3
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3C-like proteinase (EC 3.4.22.-) | protein | 306 | 24% helix, 28% strand | P0C6U8 |
Ligands and binding sites
- ZU3 · N-[(benzyloxy)carbonyl]-3-[(2,2-dimethylpropanoyl)amino]-L-alanyl-N-[(1R)-4-oxo-1-{[(3S)-2-oxopyrrolidin-3-yl]methyl}pentyl]-L-leucinamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 165 | 0.53 | 0.79 | 27 | ZU3 |
| 2 | 119 | 0.40 | 0.75 | 26 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 2ZU4 · Complex structure of SARS-CoV 3CL protease with TG-0204998 · 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 P0C6U8
- Elsewhere: RCSB PDB 2ZU4 · PDBe 2ZU4 · UniProt P0C6U8
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