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Salmonella ATPase invc with ADP

Analyse Salmonella ATPase invc with ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6RAD
Type: protein
Length: 341 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Secretory apparatus ATP synthase (associated with virulence)
UniProt: A0A0H3NGZ8
Ligands: ADP, SO4
Pockets: 2 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Secretory apparatus ATP synthase (associated with virulence)	protein	341	43% helix, 20% strand	A0A0H3NGZ8

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 7 copies · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	100	0.58	0.86	16	empty
2	109	0.44	0.78	25	empty

Compared structures

6RAD · Salmonella ATPase InvC with ADP · 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 A0A0H3NGZ8
Elsewhere: RCSB PDB 6RAD · PDBe 6RAD · UniProt A0A0H3NGZ8

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