Research workbench

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

Analyse 14-3-3 protein eta (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: 2C63
Type: protein
Length: 948 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 protein eta; Consensus peptide for 14-3-3 proteins
UniProt: Q04917
Pockets: 9 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 82% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	14-3-3 protein eta	protein	233	84% helix, 0% strand	Q04917
P, Q, R, S	Consensus peptide for 14-3-3 proteins	protein	4	0% helix, 0% strand	—

Pockets

9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	224	0.56	0.79	26	empty
2	193	0.55	0.79	28	empty
3	221	0.55	0.78	27	empty
4	179	0.55	0.80	30	empty
5	328	0.53	0.74	25	empty

Interfaces

9 interfaces between chains.

C–D · 955 Å² buried · 11 hydrogen bonds · protein-protein
A–B · 930 Å² buried · 11 hydrogen bonds · protein-protein
B–D · 382 Å² buried · 7 hydrogen bonds · protein-protein
A–P · 365 Å² buried · 9 hydrogen bonds · protein-protein
A–C · 363 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (phosphorylation).

Compared structures

2C63 · 14-3-3 Protein Eta (Human) Complexed to Peptide · the same entry in another collection · chain S against S, TM-score 1.00
Q04917 · AlphaFold monomer V2.0 prediction for 14-3-3 protein eta (Q04917) · a predicted model of the same protein · chain D against A, TM-score 0.99

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 Q04917
Elsewhere: RCSB PDB 2C63 · PDBe 2C63 · UniProt Q04917

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.