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Structure of LRRK2 after symmetry expansion

Analyse Structure of LRRK2 after symmetry expansion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7LI4
Type: protein
Length: 1,795 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Leucine-rich repeat SERINE/THREONINE-protein kinase 2
EC: 2.7.11.1, 3.6.5.-
UniProt: Q5S007
Ligands: GDP, ATP
Pockets: 20 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 27% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Leucine-rich repeat SERINE/THREONINE-protein kinase 2 (EC 2.7.11.1, 3.6.5.-)	protein	1795	27% helix, 15% strand	Q5S007

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
ATP · Adenosine-5'-triphosphate · ligand · chains A

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

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1148	0.81	0.82	114	ATP
2	1054	0.78	0.80	72	empty
3	1031	0.76	0.79	100	empty
4	906	0.76	0.79	69	empty
5	581	0.74	0.81	72	empty

Compared structures

7LI4 · Structure of LRRK2 after symmetry expansion · 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 Q5S007
Elsewhere: RCSB PDB 7LI4 · PDBe 7LI4 · UniProt Q5S007

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