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Dimerization of ELP1 is essential for elongator complex assembly

Analyse Dimerization of ELP1 is essential for elongator complex assembly in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5CQR
Type: protein
Length: 455 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Elongator complex protein 1
UniProt: O95163
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 65% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Elongator complex protein 1	protein	455	65% helix, 0% strand	O95163

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	87	0.40	0.77	18	empty

Compared structures

O95163 · AlphaFold monomer V2.0 prediction for elongator complex protein 1 (O95163) · a predicted model of the same protein · chain A against A, TM-score 0.81

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 O95163
Elsewhere: RCSB PDB 5CQR · PDBe 5CQR · UniProt O95163

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