Research workbench

14-3-3-gamma in complex with influenza NS1 C-terminal tail phosphorylated at S228

Analyse 14-3-3-gamma in complex with influenza NS1 C-terminal tail phosphorylated at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4O46
Type: protein
Length: 1,465 residues
Chains: 16
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 14-3-3 protein gamma; Nonstructural protein 1; Unidentified polymer
UniProt: P61981, Q9YP60
Ligands: UNX
Pockets: 15 · best druggability 0.71

Structure

x-ray diffraction · 11 distinct chains · 82% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	14-3-3 protein gamma	protein	235	83% helix, 0% strand	P61981
B	14-3-3 protein gamma	protein	234	83% helix, 0% strand	P61981
C, D	14-3-3 protein gamma	protein	235	83% helix, 0% strand	P61981
E	14-3-3 protein gamma	protein	236	82% helix, 0% strand	P61981
F	14-3-3 protein gamma	protein	206	84% helix, 0% strand	P61981
G, H, I, J, K	Nonstructural protein 1	protein	6	0% helix, 0% strand	Q9YP60
L	Nonstructural protein 1	protein	2	0% helix, 0% strand	Q9YP60
M	Unidentified polymer	protein	20	90% helix, 0% strand	—
N	Unidentified polymer	protein	9	78% helix, 0% strand	—
O	Unidentified polymer	protein	10	80% helix, 0% strand	—
V	Unidentified polymer	protein	13	85% helix, 0% strand	—

Ligands and binding sites

UNX · Unknown atom or ion · ion · 57 copies · chains A, C, B, D, E, K, F

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

Pockets

15 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	766	0.71	0.77	95	UNX
2	807	0.68	0.75	76	UNX
3	234	0.67	0.84	37	UNX
4	755	0.65	0.74	63	UNX
5	266	0.61	0.79	35	empty

Interfaces

13 interfaces between chains.

A–C · 1047 Å² buried · 14 hydrogen bonds · protein-protein
B–D · 1027 Å² buried · 16 hydrogen bonds · protein-protein
E–F · 892 Å² buried · 12 hydrogen bonds · protein-protein
A–B · 676 Å² buried · 8 hydrogen bonds · protein-protein
C–D · 607 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (phosphorylation).

Compared structures

4O46 · 14-3-3-gamma in complex with influenza NS1 C-terminal tail phosphorylated at S228 · the same entry in another collection · chain V against V, TM-score 1.00

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
Every structure of UniProt Q9YP60
Elsewhere: RCSB PDB 4O46 · PDBe 4O46 · UniProt P61981 · UniProt Q9YP60

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.