MolNFT v1 · #169410 · protein
Room temperature X-ray crystallography reveals catalytic cysteine in the SARS-cov-2 3CL mpro is highly reactive: insights for enzyme mechanism and drug design
6XB2: “Room temperature X-ray crystallography reveals catalytic cysteine in the SARS-cov-2 3CL mpro is highly…”. X-ray diffraction, 1 ligand (NEN). MolNFT v1 #169410 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6XB2
- Type
- protein
- Length
- 306 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DTD1
- Ligands
- NEN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 306 | — | P0DTD1 |
Ligands and binding sites
- NEN · 1-ethyl-pyrrolidine-2,5-dione · ligand · 2 copies · chains A
- DMS · Dimethyl sulfoxide · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6XB2 · Room temperature X-ray crystallography reveals catalytic cysteine in the SARS-CoV-2 3CL… · 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 6XB2 · PDBe 6XB2 · UniProt P0DTD1
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