MolNFT v1 · #181061 · protein

Human traak K+ channel fhieg mutant A198E in a K+ bound conductive conformation

7LJ5 · Isoform 2 of potassium channel subfamily K member 4: “Human traak K+ channel fhieg mutant A198E in a K+ bound conductive conformation”. X-ray diffraction, 2 ligands (K, CA), 19 pockets (best druggability 0.72). MolNFT v1 #181061 on…

PDB: 7LJ5
Type: protein
Length: 1,351 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isoform 2 of potassium channel subfamily K member 4; Anti-traak antibody 13E9 Fab…
Ligands: K, CA
Pockets: 19 · best druggability 0.72

Structure

x-ray diffraction · 5 distinct chains · 38% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Isoform 2 of potassium channel subfamily K member 4	protein	253	75% helix, 0% strand	—
B	Isoform 2 of potassium channel subfamily K member 4	protein	255	76% helix, 0% strand	—
D, F	Anti-traak antibody 13E9 Fab fragment light chain	protein	211	6% helix, 50% strand	—
E	Anti-traak antibody 13E9 Fab fragment heavy chain	protein	211	7% helix, 51% strand	—
G	Anti-traak antibody 13E9 Fab fragment heavy chain	protein	210	7% helix, 51% strand	—

Ligands and binding sites

K · Potassium ion · metal · 7 copies · chains A, B
CA · Calcium ion · metal · 3 copies · chains A, B, G

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

Pockets

19 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	993	0.72	0.76	95	CA, K
2	732	0.70	0.77	64	K
3	563	0.61	0.74	60	empty
4	265	0.57	0.78	39	empty
5	423	0.56	0.73	56	empty

Interfaces

12 interfaces between chains.

A–B · 5544 Å² buried · 46 hydrogen bonds · protein-protein
F–G · 1784 Å² buried · 16 hydrogen bonds · protein-protein
D–E · 1764 Å² buried · 19 hydrogen bonds · protein-protein
A–E · 477 Å² buried · 7 hydrogen bonds · protein-protein
B–G · 474 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 disulfide (disulfide).

Compared structures

7LJ5 · Human TRAAK K+ channel FHIEG mutant A198E in a K+ bound conductive conformation · the same entry in another collection · chain A against A, 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
Elsewhere: RCSB PDB 7LJ5 · PDBe 7LJ5

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