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CA2+ bound aplysia SLO1

Analyse CA2+ bound aplysia SLO1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TJI
Type: protein
Length: 882 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: High conductance calcium-activated potassium channel
UniProt: Q5QJC5
Ligands: PGW
Pockets: 12 · best druggability 0.75

Structure

electron microscopy · 1 distinct chain · 48% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	High conductance calcium-activated potassium channel	protein	882	48% helix, 12% strand	Q5QJC5

Ligands and binding sites

PGW · (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy) phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate · ligand · chains A

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

Pockets

12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	106	0.75	0.96	21	empty
2	680	0.72	0.79	57	empty
3	459	0.70	0.81	55	empty
4	358	0.61	0.76	47	empty
5	261	0.55	0.77	26	empty

Compared structures

5TJI · Ca2+ bound aplysia Slo1 · 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
Every structure of UniProt Q5QJC5
Elsewhere: RCSB PDB 5TJI · PDBe 5TJI · UniProt Q5QJC5

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