MolNFT v1 · #148215 · protein

14-3-3 zeta in complex with the human son of sevenless homolog 1 (SOS1)

6F08 · 14-3-3 protein ZETA/DELTA: “14-3-3 zeta in complex with the human son of sevenless homolog 1 (SOS1)”. X-ray diffraction, 5 pockets (best druggability 0.86). MolNFT v1 #148215 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 6F08
Type: protein
Length: 924 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 protein ZETA/DELTA; Son of sevenless homolog 1
UniProt: P63104, Q07889
Pockets: 5 · best druggability 0.86

Structure

x-ray diffraction · 8 distinct chains · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	14-3-3 protein ZETA/DELTA	protein	224	80% helix, 0% strand	P63104
B	14-3-3 protein ZETA/DELTA	protein	224	80% helix, 0% strand	P63104
D	Son of sevenless homolog 1	protein	9	0% helix, 0% strand	Q07889
I	14-3-3 protein ZETA/DELTA	protein	223	82% helix, 0% strand	P63104
J	14-3-3 protein ZETA/DELTA	protein	216	82% helix, 0% strand	P63104
K	Son of sevenless homolog 1	protein	10	0% helix, 0% strand	Q07889
N	Son of sevenless homolog 1	protein	8	0% helix, 0% strand	Q07889
Q	Son of sevenless homolog 1	protein	10	0% helix, 0% strand	Q07889

Ligands and binding sites

1PE · Pentaethylene glycol · additive · chains A, B

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

Pockets

5 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	1031	0.86	0.87	109	empty
2	735	0.81	0.85	76	empty
3	90	0.56	0.86	20	empty
4	102	0.55	0.84	25	empty
5	92	0.53	0.84	13	empty

Interfaces

14 interfaces between chains.

I–J · 923 Å² buried · 10 hydrogen bonds · protein-protein
A–B · 873 Å² buried · 10 hydrogen bonds · protein-protein
B–D · 783 Å² buried · 9 hydrogen bonds · protein-protein
A–Q · 775 Å² buried · 13 hydrogen bonds · protein-protein
I–K · 707 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (phosphorylation).

Compared structures

6F08 · 14-3-3 zeta in complex with the human Son of sevenless homolog 1 (SOS1) · the same entry in another collection · chain Q against Q, TM-score 1.00
P63104 · AlphaFold monomer V2.0 prediction for 14-3-3 protein ZETA/DELTA (P63104) · a predicted model of the same protein · chain I 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 P63104
Every structure of UniProt Q07889
Elsewhere: RCSB PDB 6F08 · PDBe 6F08 · UniProt P63104 · UniProt Q07889

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