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Complex organization of dengue virus E protein as revealed by 9.5 ångström cryo-EM reconstruction

Analyse Complex organization of dengue virus E protein as revealed by 9.5 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1THD
Type: protein
Length: 1,170 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Major envelope protein E
UniProt: P12823
Pockets: 1 · best druggability 0.30

Structure

electron microscopy · 1 distinct chain · 0% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Major envelope protein E	protein	390	0% helix, 0% strand	P12823

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	66	0.30	0.72	13	empty

Interfaces

3 interfaces between chains.

A–C · 104 Å² buried · 0 hydrogen bonds · protein-protein
B–C · 51 Å² buried · 0 hydrogen bonds · protein-protein
A–B · 14 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1THD · Complex organization of dengue virus E protein as revealed by 9.5 ångström cryo-EM… · 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 P12823
Elsewhere: RCSB PDB 1THD · PDBe 1THD · UniProt P12823

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