Research workbench

Legionella pneumophila LPG2603 kinase bound to IP6, MN2+, and ADP

Analyse Legionella pneumophila LPG2603 kinase bound to IP6, MN2+, and ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6VVE
Type: protein
Length: 283 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DOT/ICM T4SS effector
UniProt: A0A2S6F2W2
Ligands: IHP, ADP, MN
Pockets: 5 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DOT/ICM T4SS effector	protein	283	35% helix, 23% strand	A0A2S6F2W2

Ligands and binding sites

IHP · Inositol hexakisphosphate · ligand · chains A
ADP · Adenosine-5'-diphosphate · ligand · chains A
MN · Manganese (II) ion · metal · chains A

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

Pockets

5 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	363	0.59	0.76	50	ADP, MN
2	85	0.46	0.80	18	empty
3	88	0.41	0.78	12	empty
4	122	0.38	0.74	18	empty
5	56	0.33	0.77	16	IHP

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

6VVE · Legionella pneumophila Lpg2603 kinase bound to IP6, Mn2+, and 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 A0A2S6F2W2
Elsewhere: RCSB PDB 6VVE · PDBe 6VVE · UniProt A0A2S6F2W2

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.