MolNFT v1 · #163916 · protein
Sad structure of human survivin recovered by continuous rotation data collection and multivariate analysis of friedel pairs
6SHO · Baculoviral iap repeat-containing protein 5: “Sad structure of human survivin recovered by continuous rotation data collection and multivariate analysis of…”. X-ray diffraction, 1 ligand (ZN), 3 pockets (best druggability 0.70).…
- 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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