MolNFT v1 · #19401 · protein

14-3-3 ZETA/PHOSPHOPEPTIDE complex (mode 2)

1QJA · 14-3-3 protein zeta: “14-3-3 ZETA/PHOSPHOPEPTIDE complex (mode 2)”. X-ray diffraction, 5 pockets (best druggability 0.57). MolNFT v1 #19401 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1QJA
Type: protein
Length: 458 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 protein zeta; Phosphopeptide
UniProt: P29312
Pockets: 5 · best druggability 0.57

Structure

x-ray diffraction · 3 distinct chains · 82% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	14-3-3 protein zeta	protein	217	84% helix, 0% strand	P29312
B	14-3-3 protein zeta	protein	225	83% helix, 0% strand	P29312
Q, R	Phosphopeptide	protein	8	0% helix, 0% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	205	0.57	0.80	35	empty
2	206	0.56	0.79	31	empty
3	326	0.54	0.75	27	empty
4	65	0.26	0.73	13	empty
5	63	0.26	0.73	13	empty

Interfaces

3 interfaces between chains.

A–B · 1002 Å² buried · 12 hydrogen bonds · protein-protein
B–Q · 606 Å² buried · 11 hydrogen bonds · protein-protein
A–R · 593 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

1QJA · 14-3-3 ZETA/PHOSPHOPEPTIDE complex (mode 2) · the same entry in another collection · chain A against A, TM-score 1.00

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 P29312
Elsewhere: RCSB PDB 1QJA · PDBe 1QJA · UniProt P29312

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