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Tog-tubulin binding specificity promotes microtubule dynamics and mitotic spindle formation

Analyse Tog-tubulin binding specificity promotes microtubule dynamics and mitotic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VJC
Type: protein
Length: 508 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein mini spindles
UniProt: Q9VEZ3
Pockets: 6 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 72% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein mini spindles	protein	262	73% helix, 0% strand	Q9VEZ3
B	Protein mini spindles	protein	246	72% helix, 0% strand	Q9VEZ3

Pockets

6 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	135	0.44	0.77	23	empty
2	154	0.44	0.75	25	empty
3	79	0.33	0.75	22	empty
4	63	0.28	0.74	13	empty
5	62	0.28	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 672 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

5VJC · TOG-tubulin binding specificity promotes microtubule dynamics and mitotic spindle… · the same entry in another collection · chain A against A, TM-score 1.00
Q9VEZ3 · AlphaFold monomer V2.0 prediction for protein mini spindles (Q9VEZ3) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 Q9VEZ3
Elsewhere: RCSB PDB 5VJC · PDBe 5VJC · UniProt Q9VEZ3

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