MolNFT v1 · #172579 · protein

Structure of 14-3-3 gamma in complex with DAPK2 peptide stabilized by Fc-a

7A6Y · 14-3-3 protein gamma: “Structure of 14-3-3 gamma in complex with DAPK2 peptide stabilized by Fc-a”. X-ray diffraction, 1 ligand (FSC), 9 pockets (best druggability 0.71). MolNFT v1 #172579 on GenesisL1: 3D structure, binding sites…

PDB: 7A6Y
Type: protein
Length: 921 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 protein gamma; DAPK2 C-terminal peptide
UniProt: P61981
Ligands: FSC
Pockets: 9 · best druggability 0.71

Structure

x-ray diffraction · 7 distinct chains · 82% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	14-3-3 protein gamma	protein	226	85% helix, 0% strand	P61981
B	14-3-3 protein gamma	protein	217	81% helix, 0% strand	P61981
C	14-3-3 protein gamma	protein	225	86% helix, 0% strand	P61981
D	14-3-3 protein gamma	protein	229	81% helix, 0% strand	P61981
J, L	DAPK2 C-terminal peptide	protein	6	0% helix, 0% strand	—
K	DAPK2 C-terminal peptide	protein	7	0% helix, 0% strand	—
M	DAPK2 C-terminal peptide	protein	5	0% helix, 0% strand	—

Ligands and binding sites

FSC · Fusicoccin · ligand · 3 copies · chains A, J, B, C, L, D, M

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	841	0.71	0.76	65	empty
2	550	0.69	0.78	55	FSC
3	481	0.68	0.79	45	empty
4	205	0.58	0.80	24	FSC
5	172	0.56	0.81	23	FSC

Interfaces

9 interfaces between chains.

A–C · 1063 Å² buried · 12 hydrogen bonds · protein-protein
B–C · 653 Å² buried · 3 hydrogen bonds · protein-protein
D–M · 502 Å² buried · 19 hydrogen bonds · protein-protein
A–J · 494 Å² buried · 11 hydrogen bonds · protein-protein
B–K · 465 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (phosphorylation).

Compared structures

7A6Y · Structure of 14-3-3 gamma in complex with DAPK2 peptide stabilized by FC-A · the same entry in another collection · chain M against M, 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
Elsewhere: RCSB PDB 7A6Y · PDBe 7A6Y · UniProt P61981

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