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Structure of 14-3-3 gamma in complex with NEDD4-2 14-3-3 binding motif SER448

Analyse Structure of 14-3-3 gamma in complex with NEDD4-2 14-3-3 binding motif SER448 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ZC9
Type: protein
Length: 941 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 protein gamma; E3 ubiquitin-protein ligase NEDD4-like
EC: 2.3.2.26
UniProt: P61981, Q96PU5
Ligands: CFH
Pockets: 13 · best druggability 0.69

Structure

x-ray diffraction · 6 distinct chains · 82% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	14-3-3 protein gamma	protein	230	82% helix, 0% strand	P61981
B	14-3-3 protein gamma	protein	225	83% helix, 0% strand	P61981
C	14-3-3 protein gamma	protein	230	83% helix, 0% strand	P61981
D	14-3-3 protein gamma	protein	232	85% helix, 0% strand	P61981
E, H	E3 ubiquitin-protein ligase NEDD4-like (EC 2.3.2.26)	protein	7	0% helix, 0% strand	Q96PU5
F, G	E3 ubiquitin-protein ligase NEDD4-like (EC 2.3.2.26)	protein	5	0% helix, 0% strand	Q96PU5

Ligands and binding sites

CFH · 1,1,1,3,3,3-hexafluoropropan-2-ol · ligand · 4 copies · chains B, C, D, A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	779	0.69	0.76	57	empty
2	549	0.68	0.78	43	empty
3	86	0.68	0.93	18	CFH
4	548	0.67	0.77	46	empty
5	109	0.66	0.89	18	CFH

Interfaces

11 interfaces between chains.

B–C · 1118 Å² buried · 8 hydrogen bonds · protein-protein
A–C · 1077 Å² buried · 12 hydrogen bonds · protein-protein
B–D · 1003 Å² buried · 13 hydrogen bonds · protein-protein
A–E · 513 Å² buried · 14 hydrogen bonds · protein-protein
D–H · 453 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (phosphorylation).

Compared structures

6ZC9 · Structure of 14-3-3 gamma in complex with Nedd4-2 14-3-3 binding motif Ser448 · the same entry in another collection · chain H against H, TM-score 1.00
P61981 · AlphaFold monomer V2.0 prediction for 14-3-3 protein gamma (P61981) · 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 P61981
Every structure of UniProt Q96PU5
Elsewhere: RCSB PDB 6ZC9 · PDBe 6ZC9 · UniProt P61981 · UniProt Q96PU5

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