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The crystal structure of the cytoplasmic domain of kcsa

Analyse The crystal structure of the cytoplasmic domain of kcsa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3EFD
Type: protein
Length: 456 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fabl; Fabh; Kcsa
Pockets: 4 · best druggability 0.64

Structure

x-ray diffraction · 3 distinct chains · 10% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
L	Fabl	protein	211	5% helix, 49% strand	—
H	Fabh	protein	215	4% helix, 41% strand	—
K	Kcsa	protein	30	83% helix, 0% strand	—

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	52	0.64	0.95	21	empty
2	435	0.59	0.75	57	empty
3	60	0.38	0.79	12	empty
4	75	0.34	0.75	14	empty

Interfaces

3 interfaces between chains.

L–H · 1914 Å² buried · 17 hydrogen bonds · protein-protein
H–K · 355 Å² buried · 8 hydrogen bonds · protein-protein
L–K · 242 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

3EFD · The crystal structure of the cytoplasmic domain of KcsA · the same entry in another collection · chain L against L, 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 3EFD · PDBe 3EFD

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