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14-3-3GAMMA complexed with the N-terminal sequence of tyrosine hydroxylase (residues 1-43)

Analyse 14-3-3GAMMA complexed with the N-terminal sequence of tyrosine hydroxylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4J6S
Type: protein
Length: 990 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 protein gamma; N-terminal motif of tyrosine hydroxylase
EC: 1.14.16.2
UniProt: P61981
Pockets: 15 · best druggability 0.79

Structure

x-ray diffraction · 6 distinct chains · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	14-3-3 protein gamma	protein	237	84% helix, 0% strand	P61981
B	14-3-3 protein gamma	protein	243	81% helix, 0% strand	P61981
C	14-3-3 protein gamma	protein	236	82% helix, 0% strand	P61981
D	14-3-3 protein gamma	protein	240	81% helix, 0% strand	P61981
E	N-terminal motif of tyrosine hydroxylase (EC 1.14.16.2)	protein	7	0% helix, 0% strand	—
F, G, H	N-terminal motif of tyrosine hydroxylase (EC 1.14.16.2)	protein	9	0% helix, 0% strand	—

Pockets

15 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	1044	0.79	0.80	119	empty
2	56	0.64	0.94	18	empty
3	50	0.62	0.94	19	empty
4	217	0.57	0.79	28	empty
5	201	0.57	0.80	26	empty

Interfaces

8 interfaces between chains.

A–B · 1310 Å² buried · 12 hydrogen bonds · protein-protein
C–D · 1302 Å² buried · 12 hydrogen bonds · protein-protein
B–D · 933 Å² buried · 13 hydrogen bonds · protein-protein
A–C · 769 Å² buried · 15 hydrogen bonds · protein-protein
C–G · 662 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (phosphorylation).

Compared structures

4J6S · 14-3-3gamma complexed with the N-terminal sequence of tyrosine hydroxylase (residues 1-43) · the same entry in another collection · chain F against F, TM-score 1.00
P61981 · AlphaFold monomer V2.0 prediction for 14-3-3 protein gamma (P61981) · a predicted model of the same protein · chain C 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 P61981
Elsewhere: RCSB PDB 4J6S · PDBe 4J6S · UniProt P61981

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