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Structural basis for the interaction of 14-3-3BETA with tricarboxylic acid cycle intermediate malate

Analyse Structural basis for the interaction of 14-3-3BETA with tricarboxylic acid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5WFX
Type: protein
Length: 464 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 protein BETA/ALPHA
UniProt: Q9CQV8
Pockets: 3 · best druggability 0.50

Structure

x-ray diffraction · 2 distinct chains · 82% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	14-3-3 protein BETA/ALPHA	protein	233	83% helix, 0% strand	Q9CQV8
B	14-3-3 protein BETA/ALPHA	protein	231	81% helix, 0% strand	Q9CQV8

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	259	0.50	0.75	27	empty
2	152	0.45	0.75	21	empty
3	92	0.36	0.75	18	empty

Interfaces

1 interface between chains.

A–B · 1033 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

5WFX · Structural basis for the interaction of 14-3-3beta with Tricarboxylic Acid Cycle… · the same entry in another collection · chain B against B, TM-score 1.00
Q9CQV8 · AlphaFold monomer V2.0 prediction for 14-3-3 protein BETA/ALPHA (Q9CQV8) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9CQV8
Elsewhere: RCSB PDB 5WFX · PDBe 5WFX · UniProt Q9CQV8

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