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Structure of the hetero-tetramer complex between precursor membrane protein fragment (pr) and envelope protein (E) from tick-borne encephalitis virus

Analyse Structure of the hetero-tetramer complex between precursor membrane protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7QRE
Type: protein
Length: 480 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Genome polyprotein; Envelope protein E
UniProt: P14336
Ligands: SO4
Pockets: 3 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
D	Genome polyprotein	protein	80	4% helix, 54% strand	P14336
A	Envelope protein E	protein	400	8% helix, 47% strand	P14336

Ligands and binding sites

SO4 · Sulfate ion · ion · 8 copies · chains A
ACT · Acetate ion · additive · 2 copies · chains D, A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	131	0.60	0.85	28	empty
2	82	0.35	0.75	20	SO4
3	81	0.32	0.74	17	empty

Interfaces

1 interface between chains.

D–A · 894 Å² buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 disulfide (disulfide).

Compared structures

7QRE · Structure of the hetero-tetramer complex between precursor membrane protein fragment (pr)… · the same entry in another collection · chain D against D, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P14336
Elsewhere: RCSB PDB 7QRE · PDBe 7QRE · UniProt P14336

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