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Human 14-3-3 sigma fused to the aanat peptide including phosphoserine- 205

Analyse Human 14-3-3 sigma fused to the aanat peptide including phosphoserine- 205 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6T80
Type: protein
Length: 933 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 protein sigma; Aanat peptide
UniProt: P31947
Pockets: 8 · best druggability 0.70

Structure

x-ray diffraction · 7 distinct chains · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	14-3-3 protein sigma	protein	233	80% helix, 0% strand	P31947
B	14-3-3 protein sigma	protein	228	79% helix, 0% strand	P31947
C	14-3-3 protein sigma	protein	220	80% helix, 0% strand	P31947
D	14-3-3 protein sigma	protein	226	80% helix, 0% strand	P31947
E	Aanat peptide	protein	6	0% helix, 0% strand	—
F, G	Aanat peptide	protein	7	0% helix, 0% strand	—
H	Aanat peptide	protein	6	0% helix, 0% strand	—

Pockets

8 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	938	0.70	0.75	68	empty
2	164	0.64	0.85	24	empty
3	211	0.61	0.81	25	empty
4	342	0.59	0.77	26	empty
5	200	0.59	0.81	21	empty

Interfaces

9 interfaces between chains.

A–B · 1086 Å² buried · 15 hydrogen bonds · protein-protein
C–D · 1022 Å² buried · 14 hydrogen bonds · protein-protein
C–E · 542 Å² buried · 21 hydrogen bonds · protein-protein
D–F · 520 Å² buried · 17 hydrogen bonds · protein-protein
A–G · 499 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (phosphorylation).

Compared structures

6T80 · Human 14-3-3 sigma fused to the AANAT peptide including phosphoserine-205 · the same entry in another collection · chain H against H, TM-score 1.00
P31947 · AlphaFold monomer V2.0 prediction for 14-3-3 protein sigma (P31947) · a predicted model of the same protein · chain B 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 P31947
Elsewhere: RCSB PDB 6T80 · PDBe 6T80 · UniProt P31947

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