Research workbench
Crystal structure of borealin (20-78) bound to survivin (1-120)
Analyse Crystal structure of borealin (20-78) bound to survivin (1-120) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RAX
- Type
- protein
- Length
- 519 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Baculoviral iap repeat-containing protein 5; Borealin
- UniProt
- O15392, Q53HL2
- Ligands
- ZN
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E, X | Baculoviral iap repeat-containing protein 5 | protein | 115 | 39% helix, 8% strand | O15392 |
| B, F, Y | Borealin | protein | 58 | 76% helix, 2% strand | Q53HL2 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A, E, X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 422 | 0.57 | 0.74 | 40 | empty |
| 2 | 58 | 0.54 | 0.88 | 16 | empty |
| 3 | 139 | 0.53 | 0.81 | 31 | empty |
| 4 | 64 | 0.33 | 0.75 | 14 | empty |
Interfaces
8 interfaces between chains.
- B–F · 1138 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 948 Ų buried · 11 hydrogen bonds · protein-protein
- E–F · 940 Ų buried · 11 hydrogen bonds · protein-protein
- X–Y · 926 Ų buried · 11 hydrogen bonds · protein-protein
- B–E · 464 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2RAX · Crystal structure of Borealin (20-78) bound to Survivin (1-120) · the same entry in another collection · chain Y against Y, TM-score 1.00
- O15392 · AlphaFold monomer V2.0 prediction for baculoviral iap repeat- containing protein 5… · a predicted model of the same protein · chain E against A, TM-score 0.97
- Q53HL2 · AlphaFold monomer V2.0 prediction for borealin (Q53HL2) · a predicted model of the same protein · chain F against A, TM-score 0.85
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 O15392
- Every structure of UniProt Q53HL2
- Elsewhere: RCSB PDB 2RAX · PDBe 2RAX · UniProt O15392 · UniProt Q53HL2
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