Research workbench

Structural basis of microtubule plus end tracking by XMAP215, clip-170 and EB1

Analyse Structural basis of microtubule plus end tracking by XMAP215, clip-170 and EB1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2QK1
Type: protein
Length: 247 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein STU2
UniProt: P46675
Pockets: 1 · best druggability 0.28

Structure

x-ray diffraction · 1 distinct chain · 70% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein STU2	protein	247	70% helix, 1% strand	P46675

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	50	0.28	0.75	11	empty

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

2QK1 · Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1 · the same entry in another collection · chain A against A, TM-score 1.00
P46675 · AlphaFold monomer V2.0 prediction for protein STU2 (P46675) · 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 P46675
Elsewhere: RCSB PDB 2QK1 · PDBe 2QK1 · UniProt P46675

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