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14-3-3 protein epsilon (human) complexed to peptide

Analyse 14-3-3 protein epsilon (human) complexed to peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BR9
Type: protein
Length: 236 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 protein epsilon; Consensus peptide for 14-3-3 proteins
UniProt: P62258
Pockets: 3 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 84% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	14-3-3 protein epsilon	protein	230	86% helix, 0% strand	P62258
P	Consensus peptide for 14-3-3 proteins	protein	6	0% helix, 0% strand	—

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	164	0.54	0.80	20	empty
2	64	0.41	0.80	14	empty
3	65	0.32	0.76	17	empty

Interfaces

1 interface between chains.

A–P · 508 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

2BR9 · 14-3-3 Protein Epsilon (Human) Complexed to Peptide · the same entry in another collection · chain A against A, TM-score 1.00
P62258 · AlphaFold monomer V2.0 prediction for 14-3-3 protein epsilon (P62258) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P62258
Elsewhere: RCSB PDB 2BR9 · PDBe 2BR9 · UniProt P62258

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