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Non-square conformation of ktra A80P mutant ring with bound ATP

Analyse Non-square conformation of ktra A80P mutant ring with bound ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6S5E
Type: protein
Length: 1,736 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ktr system potassium uptake protein a
UniProt: O32080
Ligands: ATP
Pockets: 20 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H	Ktr system potassium uptake protein a	protein	217	38% helix, 29% strand	O32080

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 8 copies · chains A, B, C, D, E, F, G, H

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

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1140	0.71	0.75	88	empty
2	820	0.69	0.75	86	empty
3	412	0.65	0.79	42	empty
4	437	0.63	0.77	35	empty
5	435	0.62	0.76	39	empty

Interfaces

16 interfaces between chains.

G–H · 2429 Å² buried · 17 hydrogen bonds · protein-protein
E–F · 2410 Å² buried · 14 hydrogen bonds · protein-protein
C–D · 2390 Å² buried · 14 hydrogen bonds · protein-protein
A–B · 2332 Å² buried · 15 hydrogen bonds · protein-protein
D–F · 268 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

6S5E · Non-square conformation of KtrA A80P mutant ring with bound ATP · the same entry in another collection · chain H against H, TM-score 1.00
O32080 · AlphaFold monomer V2.0 prediction for ktr system potassium uptake protein a (O32080) · a predicted model of the same protein · chain A against A, TM-score 0.98

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
Elsewhere: RCSB PDB 6S5E · PDBe 6S5E · UniProt O32080

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