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Structure of prrsv apo-NSP11 at 2.16A

Analyse Structure of prrsv apo-NSP11 at 2.16A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5EYI
Type: protein
Length: 433 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Non-structural protein 11
UniProt: Q9YN02
Ligands: SO4, CL
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 15% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Non-structural protein 11	protein	223	16% helix, 36% strand	Q9YN02
B	Non-structural protein 11	protein	210	15% helix, 31% strand	Q9YN02

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A
CL · Chloride ion · ion · chains A
PG0 · 2-(2-methoxyethoxy)ethanol · additive · 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	467	0.68	0.79	59	CL

Interfaces

1 interface between chains.

A–B · 747 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

5EYI · Structure of PRRSV apo-NSP11 at 2.16A · the same entry in another collection · chain B against B, 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 Q9YN02
Elsewhere: RCSB PDB 5EYI · PDBe 5EYI · UniProt Q9YN02

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