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Integrative in situ structure of parkinsons disease-linked human LRRK2

Analyse Integrative in situ structure of parkinsons disease-linked human LRRK2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6XR4
Type: protein
Length: 2,080 residues
Chains: 2
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
Pockets: 3 · best druggability 0.31

Structure

electron microscopy · 1 distinct chain · 0% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Leucine-rich repeat SERINE/THREONINE-protein kinase 2 (EC 2.7.11.1, 3.6.5.-)	protein	1040	0% helix, 0% strand	Q5S007

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	68	0.31	0.72	24	empty
2	64	0.30	0.72	21	empty
3	59	0.29	0.72	24	empty

Interfaces

1 interface between chains.

A–B · 33 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6XR4 · Integrative in situ structure of Parkinsons disease-linked human LRRK2 · the same entry in another collection · chain A against A, TM-score 1.00
Q5S007 · AlphaFold monomer V2.0 prediction for leucine-rich repeat SERINE/THREONINE-protein kinase… · a predicted model of the same protein · chain A against A, TM-score 0.75

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 6XR4 · PDBe 6XR4 · UniProt Q5S007

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