MolNFT v1 · #150126 · protein

Structure of 14-3-3 gamma in complex with caspase-2 14-3-3 binding motif SER139

6GKF · 14-3-3 protein gamma: “Structure of 14-3-3 gamma in complex with caspase-2 14-3-3 binding motif SER139”. X-ray diffraction, 20 pockets (best druggability 0.73). MolNFT v1 #150126 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 6GKF
Type: protein
Length: 1,847 residues
Chains: 16
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 protein gamma; Caspase-2
EC: 3.4.22.55
UniProt: P61981
Pockets: 20 · best druggability 0.73

Structure

x-ray diffraction · 11 distinct chains · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	14-3-3 protein gamma	protein	223	83% helix, 0% strand	P61981
C	14-3-3 protein gamma	protein	228	84% helix, 0% strand	P61981
E	14-3-3 protein gamma	protein	233	81% helix, 0% strand	P61981
G	14-3-3 protein gamma	protein	217	82% helix, 0% strand	P61981
B	14-3-3 protein gamma	protein	227	82% helix, 0% strand	P61981
D	14-3-3 protein gamma	protein	227	81% helix, 0% strand	P61981
F	14-3-3 protein gamma	protein	213	84% helix, 0% strand	P61981
H	14-3-3 protein gamma	protein	220	82% helix, 0% strand	P61981
I, K, M, O, P	Caspase-2 (EC 3.4.22.55)	protein	8	0% helix, 0% strand	—
J	Caspase-2 (EC 3.4.22.55)	protein	7	0% helix, 0% strand	—
L, N	Caspase-2 (EC 3.4.22.55)	protein	6	0% helix, 0% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	239	0.73	0.87	43	empty
2	889	0.71	0.76	81	empty
3	518	0.66	0.77	48	empty
4	684	0.63	0.73	64	empty
5	204	0.60	0.81	37	empty

Interfaces

18 interfaces between chains.

C–D · 1032 Å² buried · 12 hydrogen bonds · protein-protein
G–H · 1007 Å² buried · 12 hydrogen bonds · protein-protein
E–F · 967 Å² buried · 12 hydrogen bonds · protein-protein
A–B · 963 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 783 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (phosphorylation).

Compared structures

6GKF · Structure of 14-3-3 gamma in complex with caspase-2 14-3-3 binding motif Ser139 · the same entry in another collection · chain P against P, 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 P61981
Elsewhere: RCSB PDB 6GKF · PDBe 6GKF · UniProt P61981

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