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Human coronavirus 229E non structural protein 9 CYS69ALA mutant (NSP9)

Analyse Human coronavirus 229E non structural protein 9 CYS69ALA mutant (NSP9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2J98
Type: protein
Length: 208 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Replicase polyprotein 1AB
UniProt: P0C6U2
Pockets: 2 · best druggability 0.36

Structure

x-ray diffraction · 2 distinct chains · 16% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Replicase polyprotein 1AB	protein	106	16% helix, 49% strand	P0C6U2
B	Replicase polyprotein 1AB	protein	102	17% helix, 50% strand	P0C6U2

Ligands and binding sites

DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · 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	62	0.36	0.77	14	empty
2	54	0.36	0.79	16	DTT

Interfaces

1 interface between chains.

A–B · 634 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

2J98 · Human coronavirus 229E non structural protein 9 cys69ala mutant (Nsp9) · 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 P0C6U2
Elsewhere: RCSB PDB 2J98 · PDBe 2J98 · UniProt P0C6U2

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