Research workbench

14-3-3 protein tau isoform

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

PDB: 5IQP
Type: protein
Length: 459 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 protein theta
UniProt: P27348
Ligands: SO4
Pockets: 3 · best druggability 0.55

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	14-3-3 protein theta	protein	230	82% helix, 0% strand	P27348
B	14-3-3 protein theta	protein	229	83% helix, 0% strand	P27348

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	295	0.55	0.75	27	SO4
2	324	0.53	0.74	27	empty
3	242	0.51	0.76	29	SO4

Interfaces

1 interface between chains.

A–B · 1027 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

5IQP · 14-3-3 protein tau isoform · the same entry in another collection · chain A against A, TM-score 1.00
P27348 · AlphaFold monomer V2.0 prediction for 14-3-3 protein theta (P27348) · a predicted model of the same protein · chain B 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 P27348
Elsewhere: RCSB PDB 5IQP · PDBe 5IQP · UniProt P27348

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