Research workbench

B-RAF:14-3-3 complex

Analyse B-RAF:14-3-3 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UAN
Type: protein
Length: 1,007 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 zeta; SERINE/THREONINE-protein kinase B-RAF
EC: 2.7.11.1
UniProt: A0A068JLL8, P15056
Pockets: 20 · best druggability 0.76

Structure

electron microscopy · 4 distinct chains · 49% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	14-3-3 zeta	protein	231	75% helix, 0% strand	A0A068JLL8
Z	14-3-3 zeta	protein	230	74% helix, 0% strand	A0A068JLL8
B	SERINE/THREONINE-protein kinase B-RAF (EC 2.7.11.1)	protein	261	31% helix, 10% strand	P15056
C	SERINE/THREONINE-protein kinase B-RAF (EC 2.7.11.1)	protein	285	24% helix, 13% strand	P15056

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	765	0.76	0.80	101	empty
2	96	0.74	0.95	24	empty
3	723	0.68	0.76	88	empty
4	62	0.67	0.95	18	empty
5	387	0.66	0.80	42	empty

Interfaces

5 interfaces between chains.

B–C · 1986 Å² buried · 23 hydrogen bonds · protein-protein
A–Z · 961 Å² buried · 5 hydrogen bonds · protein-protein
Z–B · 923 Å² buried · 7 hydrogen bonds · protein-protein
A–C · 747 Å² buried · 6 hydrogen bonds · protein-protein
Z–C · 133 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

6UAN · B-Raf:14-3-3 complex · the same entry in another collection · chain A against A, TM-score 1.00
P15056 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase B-RAF (P15056) · a predicted model of the same protein · chain C against A, TM-score 0.88

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 A0A068JLL8
Every structure of UniProt P15056
Elsewhere: RCSB PDB 6UAN · PDBe 6UAN · UniProt A0A068JLL8 · UniProt P15056

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