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The structure of the C-terminal domain of VIK1 has a motor domain fold but lacks a nucleotide-binding site.

Analyse The structure of the C-terminal domain of VIK1 has a motor domain fold but… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O0A
Type: protein
Length: 269 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: S.CEREVISIAE chromosome xvi reading frame orf YPL253C
UniProt: Q12045
Pockets: 2 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	S.CEREVISIAE chromosome xvi reading frame orf YPL253C	protein	269	39% helix, 29% strand	Q12045

Ligands and binding sites

EDO · 1,2-ethanediol · additive · chains A

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

Pockets

2 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	59	0.34	0.78	19	empty
2	65	0.28	0.73	18	empty

Compared structures

2O0A · The structure of the C-terminal domain of Vik1 has a motor domain fold but lacks a… · the same entry in another collection · chain A against A, TM-score 1.00
Q12045 · AlphaFold monomer V2.0 prediction for spindle pole body-associated protein VIK1 (Q12045) · a predicted model of the same protein · chain A 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 Q12045
Elsewhere: RCSB PDB 2O0A · PDBe 2O0A · UniProt Q12045

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