Research workbench

Crystal structure of SARS-cov-2 NSP3 macrodomain at pH 7 (P43 crystal form)

Analyse Crystal structure of SARS-cov-2 NSP3 macrodomain at pH 7 (P43 crystal form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7TWP
Type: protein
Length: 334 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Non-structural protein 3
EC: 3.4.19.121, 3.4.22.-
UniProt: P0DTD1
Pockets: 4 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Non-structural protein 3 (EC 3.4.19.121, 3.4.22.-)	protein	167	40% helix, 19% strand	P0DTD1

Ligands and binding sites

ACT · Acetate ion · additive · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	426	0.65	0.78	33	empty
2	156	0.54	0.80	32	ACT
3	152	0.50	0.78	25	empty
4	50	0.28	0.75	13	empty

Interfaces

1 interface between chains.

A–B · 514 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

7TWP · Crystal structure of SARS-CoV-2 NSP3 macrodomain at pH 7 (P43 crystal form) · 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 7TWP · PDBe 7TWP · UniProt P0DTD1

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.