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BUB3 complex with MAD3 (BUBR1) glebs motif

Analyse BUB3 complex with MAD3 (BUBR1) glebs motif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2I3T
Type: protein
Length: 1,484 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell cycle arrest protein; Spindle assembly checkpoint component
UniProt: P26449, P47074
Pockets: 13 · best druggability 0.71

Structure

x-ray diffraction · 3 distinct chains · 9% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E, G	Cell cycle arrest protein	protein	334	4% helix, 53% strand	P26449
B, F, H	Spindle assembly checkpoint component	protein	35	31% helix, 14% strand	P47074
D	Spindle assembly checkpoint component	protein	43	28% helix, 9% strand	P47074

Pockets

13 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.71	0.98	20	empty
2	455	0.70	0.80	43	empty
3	444	0.69	0.80	42	empty
4	414	0.68	0.81	38	empty
5	452	0.68	0.80	42	empty

Interfaces

10 interfaces between chains.

C–D · 1854 Å² buried · 24 hydrogen bonds · protein-protein
E–F · 1790 Å² buried · 27 hydrogen bonds · protein-protein
G–H · 1782 Å² buried · 27 hydrogen bonds · protein-protein
A–B · 1778 Å² buried · 33 hydrogen bonds · protein-protein
A–G · 652 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

2I3T · Bub3 complex with Mad3 (BubR1) GLEBS motif · the same entry in another collection · chain H against H, 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 C against A, TM-score 0.96

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
Every structure of UniProt P47074
Elsewhere: RCSB PDB 2I3T · PDBe 2I3T · UniProt P26449 · UniProt P47074

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