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X-ray crystal structure of the E2 domain of C. elegans APL-1

Analyse X-ray crystal structure of the E2 domain of C. elegans APL-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3K66
Type: protein
Length: 217 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.7
Source: Caenorhabditis elegans
Molecule: Beta-amyloid-like protein
UniProt: Q10651
Pockets: 3 · best druggability 0.49

Structure

x-ray diffraction · resolution 2.7 · 1 distinct chain · 85% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-amyloid-like protein	protein	217	85% helix, 0% strand	Q10651

Pockets

3 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	113	0.49	0.80	17	empty
2	113	0.39	0.75	17	empty
3	54	0.25	0.72	18	empty

Compared structures

3K66 · X-ray crystal structure of the E2 domain of C. elegans apl-1 · the same entry in another collection · chain A against A, TM-score 1.00
Q10651 · AlphaFold monomer V2.0 prediction for amyloid-beta-like protein (Q10651) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q10651
Elsewhere: RCSB PDB 3K66 · PDBe 3K66 · UniProt Q10651

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