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Structural basis for altered function in the common mutants of human apolipoprotein-E

Analyse Structural basis for altered function in the common mutants of human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LE2
Type: protein
Length: 144 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Apolipoprotein E2
UniProt: P02649
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 83% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Apolipoprotein E2	protein	144	83% helix, 0% strand	P02649

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	60	0.29	0.75	16	empty

Compared structures

1LE2 · Structural basis for altered function in the common mutants of human apolipoprotein-E · the same entry in another collection · chain A against A, TM-score 1.00
P02649 · AlphaFold monomer V2.0 prediction for apolipoprotein E (P02649) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P02649
Elsewhere: RCSB PDB 1LE2 · PDBe 1LE2 · UniProt P02649

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