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AKT1 K+ channel from a. thaliana in MSP2N2 lipid nanodisc

Analyse AKT1 K+ channel from a. thaliana in MSP2N2 lipid nanodisc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7T4X
Type: protein
Length: 1,778 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Potassium channel AKT1
UniProt: Q38998
Ligands: PTY, K
Pockets: 20 · best druggability 0.82

Structure

electron microscopy · 2 distinct chains · 62% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Potassium channel AKT1	protein	439	61% helix, 10% strand	Q38998
B, D	Potassium channel AKT1	protein	450	63% helix, 9% strand	Q38998

Ligands and binding sites

PTY · Phosphatidylethanolamine · ligand · 2 copies · chains A, B, C, D
K · Potassium ion · metal · 5 copies · chains A, B, C, D

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	636	0.82	0.86	75	empty
2	721	0.72	0.78	52	empty
3	688	0.71	0.78	51	empty
4	925	0.70	0.75	90	empty
5	477	0.65	0.77	29	empty

Interfaces

6 interfaces between chains.

C–D · 2679 Å² buried · 16 hydrogen bonds · protein-protein
A–B · 2675 Å² buried · 16 hydrogen bonds · protein-protein
A–D · 2480 Å² buried · 20 hydrogen bonds · protein-protein
B–C · 2476 Å² buried · 20 hydrogen bonds · protein-protein
B–D · 64 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

7T4X · AKT1 K+ channel from A. thaliana in MSP2N2 lipid nanodisc · the same entry in another collection · chain D against D, TM-score 1.00
Q38998 · AlphaFold monomer V2.0 prediction for potassium channel AKT1 (Q38998) · a predicted model of the same protein · chain A against A, TM-score 0.88

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 Q38998
Elsewhere: RCSB PDB 7T4X · PDBe 7T4X · UniProt Q38998

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