Research workbench
Crystal structure of the borealin-survivin complex
Analyse Crystal structure of the borealin-survivin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RAW
- Type
- protein
- Length
- 193 residues
- Chains
- 2
- 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
- 1 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 59% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Baculoviral iap repeat-containing protein 5 | protein | 137 | 50% helix, 7% strand | O15392 |
| B | Borealin | protein | 56 | 80% helix, 2% strand | Q53HL2 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.41 | 0.78 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1428 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 2RAW · Crystal structure of the Borealin-Survivin complex · the same entry in another collection · chain A against A, 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 A against A, TM-score 0.96
- Q53HL2 · AlphaFold monomer V2.0 prediction for borealin (Q53HL2) · a predicted model of the same protein · chain B 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 2RAW · PDBe 2RAW · UniProt O15392 · UniProt Q53HL2
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