MolNFT v1 · #78901 · protein

Crystal structure of SARS coronavirus main protease complexed with cm- ff-H (soaking)

3SN8 · 3C-like proteinase: “Crystal structure of SARS coronavirus main protease complexed with cm- ff-H (soaking)”. X-ray diffraction, 1 ligand (S89), 2 pockets (best druggability 0.47). MolNFT v1 #78901 on GenesisL1: 3D structure, binding…

PDB: 3SN8
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: S89
Pockets: 2 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3C-like proteinase (EC 3.4.22.-)	protein	306	26% helix, 28% strand	P0C6U8

Ligands and binding sites

S89 · N-[(2S)-1-hydroxy-3-phenylpropan-2-yl]-Nalpha-[(2E)-3-phenylprop-2-enoyl]-L-phenylalaninamide · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	180	0.47	0.76	29	S89
2	125	0.41	0.75	23	empty

Modifications

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

Compared structures

3SN8 · Crystal structure of SARS coronavirus main protease complexed with Cm-FF-H (soaking) · 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 3SN8 · PDBe 3SN8 · UniProt P0C6U8

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