Research workbench
BUB3 complex with BUB1 glebs motif
Analyse BUB3 complex with BUB1 glebs motif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2I3S
- Type
- protein
- Length
- 1,102 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P26449, P41695
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 334 | — | P26449 |
| B, D, F | — | protein | 36 | — | P41695 |
| C | — | protein | 328 | — | P26449 |
| E | — | protein | 332 | — | P26449 |
Compared structures
- 2I3S · Bub3 complex with Bub1 GLEBS motif · the same entry in another collection · chain D against D, 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 0.97
- P41695 · AlphaFold monomer V2.0 prediction for checkpoint SERINE/THREONINE- protein kinase BUB1… · a predicted model of the same protein · chain B against A, TM-score 0.73
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 P41695
- Elsewhere: RCSB PDB 2I3S · PDBe 2I3S · UniProt P26449 · UniProt P41695
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