Research workbench
Crystal structure of human survivin bound to histone H3 phosphorylated on threonine-3.
Analyse Crystal structure of human survivin bound to histone H3 phosphorylated on… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UEC
- Type
- protein
- Length
- 142 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Baculoviral iap repeat-containing protein 5; N-terminal fragment of histone H3
- UniProt
- O15392
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Baculoviral iap repeat-containing protein 5 | protein | 138 | 52% helix, 7% strand | O15392 |
| B | N-terminal fragment of histone H3 | protein | 4 | 0% helix, 50% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
- PG4 · Tetraethylene glycol · additive · chains A
- 1PE · Pentaethylene glycol · additive · chains A
- ACT · Acetate ion · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 98 | 0.52 | 0.83 | 19 | 1PE |
Interfaces
1 interface between chains.
- A–B · 423 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 3UEC · Crystal structure of human Survivin bound to histone H3 phosphorylated on threonine-3. · 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 0.94
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 3UEC · PDBe 3UEC · UniProt O15392
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