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Crystal structure of human 14-3-3 protein beta in complex with cftr peptide PS753PS768 and ppi stabilizer CY007424

Analyse Crystal structure of human 14-3-3 protein beta in complex with cftr peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7QI1
Type: protein
Length: 973 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 protein BETA/ALPHA; Cystic fibrosis transmembrane conductance regulator
EC: 3.6.3.49
UniProt: S7N159, P13569
Ligands: ARG, Q95, TYR
Pockets: 9 · best druggability 0.76

Structure

x-ray diffraction · 6 distinct chains · 80% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	14-3-3 protein BETA/ALPHA	protein	234	83% helix, 0% strand	S7N159
B	14-3-3 protein BETA/ALPHA	protein	232	84% helix, 0% strand	S7N159
F	Cystic fibrosis transmembrane conductance regulator (EC 3.6.3.49)	protein	22	0% helix, 0% strand	P13569
E	Cystic fibrosis transmembrane conductance regulator (EC 3.6.3.49)	protein	16	0% helix, 6% strand	P13569
C	14-3-3 protein BETA/ALPHA	protein	236	82% helix, 0% strand	S7N159
D	14-3-3 protein BETA/ALPHA	protein	233	83% helix, 0% strand	S7N159

Ligands and binding sites

ARG · Arginine · ligand · 2 copies · chains A, C, B
Q95 · [2-(2-methylphenyl)sulfanylphenyl]methanamine · ligand · 2 copies · chains A, F, C, B
TYR · Tyrosine · ligand · chains A, F, C

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

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1017	0.76	0.79	86	ARG, Q95, TYR
2	434	0.72	0.82	52	empty
3	764	0.70	0.77	59	empty
4	406	0.62	0.76	47	empty
5	201	0.49	0.75	28	empty

Interfaces

10 interfaces between chains.

A–B · 1078 Å² buried · 11 hydrogen bonds · protein-protein
C–D · 1027 Å² buried · 11 hydrogen bonds · protein-protein
A–F · 998 Å² buried · 17 hydrogen bonds · protein-protein
F–D · 830 Å² buried · 18 hydrogen bonds · protein-protein
B–E · 773 Å² buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified, 2 covalent (phosphorylation, covalent ligand).

Compared structures

7QI1 · Crystal structure of human 14-3-3 protein beta in complex with CFTR peptide pS753pS768… · the same entry in another collection · chain D against D, TM-score 1.00
P13569 · AlphaFold monomer V2.0 prediction for cystic fibrosis transmembrane conductance regulator… · a predicted model of the same protein · chain E against A, TM-score 0.29

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 S7N159
Every structure of UniProt P13569
Elsewhere: RCSB PDB 7QI1 · PDBe 7QI1 · UniProt S7N159 · UniProt P13569

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