Research workbench

Open and conductive conformation of kcsa-T75A mutant

Analyse Open and conductive conformation of kcsa-T75A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6BY3
Type: protein
Length: 527 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Antibody heavy chain; Antibody light chain; PH-gated potassium channel kcsa
UniProt: P0A333
Ligands: F09, DGA, K
Pockets: 6 · best druggability 0.68

Structure

x-ray diffraction · 3 distinct chains · 17% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Antibody heavy chain	protein	219	3% helix, 49% strand	—
B	Antibody light chain	protein	212	5% helix, 51% strand	—
C	PH-gated potassium channel kcsa	protein	96	74% helix, 0% strand	P0A333

Ligands and binding sites

F09 · Nonan-1-ol · ligand · chains A, C
DGA · Diacyl glycerol · ligand · chains C
K · Potassium ion · metal · 6 copies · chains C

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

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	750	0.68	0.76	57	empty
2	55	0.53	0.89	22	empty
3	243	0.53	0.76	37	empty
4	66	0.51	0.85	14	empty
5	66	0.47	0.84	16	empty

Interfaces

3 interfaces between chains.

A–B · 1797 Å² buried · 22 hydrogen bonds · protein-protein
A–C · 481 Å² buried · 9 hydrogen bonds · protein-protein
B–C · 437 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

6BY3 · Open and conductive conformation of KcsA-T75A mutant · the same entry in another collection · chain A against A, TM-score 1.00
P0A333 · AlphaFold monomer V2.0 prediction for pH-gated potassium channel kcsa (P0A333) · a predicted model of the same protein · chain C against A, TM-score 0.81

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 P0A333
Elsewhere: RCSB PDB 6BY3 · PDBe 6BY3 · UniProt P0A333

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