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Ktrab potassium transporter from bacillus subtilis

Analyse Ktrab potassium transporter from bacillus subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4J7C
Type: protein
Length: 3,448 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ktr system potassium uptake protein a; Ktr system potassium uptake protein B
UniProt: O32080, O32081
Ligands: ATP, K
Pockets: 20 · best druggability 0.88

Structure

x-ray diffraction · 3 distinct chains · 50% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E, G	Ktr system potassium uptake protein a	protein	216	37% helix, 29% strand	O32080
B, D, F, H	Ktr system potassium uptake protein a	protein	217	35% helix, 28% strand	O32080
I, J, K, L	Ktr system potassium uptake protein B	protein	429	65% helix, 2% strand	O32081

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 8 copies · chains A, B, C, D, E, F, G, H
K · Potassium ion · metal · 4 copies · chains I, J, K, L

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	552	0.88	0.92	45	empty
2	573	0.87	0.91	49	empty
3	792	0.76	0.80	78	empty
4	721	0.76	0.81	81	empty
5	744	0.75	0.80	87	empty

Interfaces

34 interfaces between chains.

I–J · 3767 Å² buried · 39 hydrogen bonds · protein-protein
K–L · 3721 Å² buried · 36 hydrogen bonds · protein-protein
G–H · 2495 Å² buried · 12 hydrogen bonds · protein-protein
C–D · 2462 Å² buried · 12 hydrogen bonds · protein-protein
A–B · 2448 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

4J7C · KtrAB potassium transporter from Bacillus subtilis · 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
Every structure of UniProt O32080
Every structure of UniProt O32081
Elsewhere: RCSB PDB 4J7C · PDBe 4J7C · UniProt O32080 · UniProt O32081

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