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Bacterial sodium channel neck 3G mutant

Analyse Bacterial sodium channel neck 3G mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HJ8
Type: protein
Length: 492 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ion transport protein
UniProt: Q0ABW0
Ligands: CA
Pockets: 3 · best druggability 0.80

Structure

x-ray diffraction · 3 distinct chains · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ion transport protein	protein	124	80% helix, 0% strand	Q0ABW0
B	Ion transport protein	protein	118	75% helix, 0% strand	Q0ABW0
C, D	Ion transport protein	protein	125	78% helix, 0% strand	Q0ABW0

Ligands and binding sites

CA · Calcium ion · metal · chains A, B, C, D

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1123	0.80	0.80	79	CA
2	269	0.62	0.80	30	empty
3	92	0.50	0.82	21	empty

Interfaces

6 interfaces between chains.

C–D · 1317 Å² buried · 11 hydrogen bonds · protein-protein
A–B · 1300 Å² buried · 11 hydrogen bonds · protein-protein
B–C · 1271 Å² buried · 11 hydrogen bonds · protein-protein
A–D · 1262 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 122 Å² buried · 0 hydrogen bonds · protein-protein

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 Q0ABW0
Elsewhere: RCSB PDB 5HJ8 · PDBe 5HJ8 · UniProt Q0ABW0

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