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Group deposition for crystallographic fragment screening of Coxsackievirus A16 (G-10) 2A protease -- Crystal structure of Coxsackievirus A16 (G-10) 2A protease in complex with Z1456069604 (A71EV2A-x0269)

Analyse Group deposition for crystallographic fragment screening of Coxsackievirus A16… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7H32
Type: protein
Length: 140 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.28
Source: Coxsackievirus A16
Molecule: Protease 2A
EC: 3.4.22.29
UniProt: Q65900
Ligands: 89W, ZN, SO4
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · resolution 1.28 · 1 distinct chain · 15% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protease 2A (EC 3.4.22.29)	protein	140	15% helix, 54% strand	Q65900

Ligands and binding sites

89W · N-[(3R)-piperidin-3-yl]benzamide · ligand · chains A
ZN · Zinc ion · metal · chains A
SO4 · Sulfate ion · ion
DMS · Dimethyl sulfoxide · additive · 3 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	90	0.42	0.78	26	empty

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Every structure of UniProt Q65900
Elsewhere: RCSB PDB 7H32 · PDBe 7H32 · UniProt Q65900

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