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Crystal structure of SARS-CoV-2 NSP3 Macrodomain in complex with ASAP-0011221-001

Analyse Crystal structure of SARS-CoV-2 NSP3 Macrodomain in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7H00
Type: protein
Length: 167 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.18
Source: Severe acute respiratory syndrome coronavirus 2
Molecule: Papain-like protease nsp3
EC: 3.4.19.12, 3.4.22.-
UniProt: P0DTD1
Ligands: A1ALQ
Pockets: 1 · best druggability 0.53

Structure

x-ray diffraction · resolution 1.18 · 1 distinct chain · 41% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Papain-like protease nsp3 (EC 3.4.19.12, 3.4.22.-)	protein	167	41% helix, 20% strand	P0DTD1

Ligands and binding sites

A1ALQ · (4M)-4-(4-{[(1S)-1-(2,3-dihydro[1,4]dioxino[2,3-b]pyridin-6-yl)-2,2-dimethylpropyl]amino}-7H-pyrrolo[2,3-d]pyrimidin-6-yl)-1-methyl-1H-pyrazole-5-carbonitrile · ligand · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	200	0.53	0.78	31	A1ALQ

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 7H00 · PDBe 7H00 · UniProt P0DTD1

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