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Electron cyro-microscopy helical reconstruction of par-3 N terminal domain

Analyse Electron cyro-microscopy helical reconstruction of par-3 N terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ZEE
Type: protein
Length: 84 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Partitioning defective 3 homolog
UniProt: Q9Z340
Pockets: 1 · best druggability 0.70

Structure

electron microscopy · 1 distinct chain · 24% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Partitioning defective 3 homolog	protein	84	24% helix, 29% strand	Q9Z340

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	66	0.70	0.96	26	empty

Compared structures

3ZEE · Electron cyro-microscopy helical reconstruction of Par-3 N terminal domain · the same entry in another collection · chain A against A, TM-score 1.00
Q9Z340 · AlphaFold monomer V2.0 prediction for partitioning defective 3 homolog (Q9Z340) · a predicted model of the same protein · chain A against A, TM-score 0.84

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 Q9Z340
Elsewhere: RCSB PDB 3ZEE · PDBe 3ZEE · UniProt Q9Z340

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