Research workbench
Sad structure of human survivin recovered by continuous rotation data collection and multivariate analysis of friedel pairs
Analyse Sad structure of human survivin recovered by continuous rotation data… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SHO
- Type
- protein
- Length
- 270 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Baculoviral iap repeat-containing protein 5
- UniProt
- O15392
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Baculoviral iap repeat-containing protein 5 | protein | 135 | 54% helix, 7% strand | O15392 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 66 | 0.70 | 0.95 | 17 | empty |
| 2 | 118 | 0.55 | 0.83 | 21 | empty |
| 3 | 111 | 0.43 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 555 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6SHO · SAD structure of Human Survivin recovered by continuous rotation data collection and… · 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 B against A, TM-score 0.97
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
- Elsewhere: RCSB PDB 6SHO · PDBe 6SHO · UniProt O15392
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