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High resolution S. cerevisiae BUB3 mitotic checkpoint protein

Analyse High resolution S. cerevisiae BUB3 mitotic checkpoint protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1YFQ
Type: protein
Length: 342 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell cycle arrest protein BUB3
UniProt: P26449
Ligands: CA
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell cycle arrest protein BUB3	protein	342	4% helix, 49% strand	P26449

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains A
ACT · Acetate ion · additive · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	494	0.69	0.79	46	CA
2	315	0.67	0.82	40	CA
3	85	0.44	0.80	20	empty
4	60	0.39	0.80	13	empty

Compared structures

1YFQ · High resolution S. cerevisiae Bub3 mitotic checkpoint protein · the same entry in another collection · chain A against A, TM-score 1.00
P26449 · AlphaFold monomer V2.0 prediction for cell cycle arrest protein BUB3 (P26449) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P26449
Elsewhere: RCSB PDB 1YFQ · PDBe 1YFQ · UniProt P26449

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