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Crystal structure of SARS coronavirus 3CL protease inhibitor complex

Analyse Crystal structure of SARS coronavirus 3CL protease inhibitor complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GX4
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: P59641
Ligands: NOL
Pockets: 3 · 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	P59641

Ligands and binding sites

NOL · N-[(benzyloxy)carbonyl]-O-(tert-butyl)-L-threonyl-3-cyclohexyl-N-[(1S)-2-hydroxy-1-{[(3S)-2-oxopyrrolidin-3-yl]methyl}ethyl]-L-alaninamide · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	212	0.53	0.78	30	NOL
2	57	0.30	0.75	13	empty
3	50	0.27	0.74	13	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

2GX4 · Crystal structure of SARS coronavirus 3CL protease inhibitor complex · 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 P59641
Elsewhere: RCSB PDB 2GX4 · PDBe 2GX4 · UniProt P59641

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