MolNFT v1 · #85061 · protein
Crystal structure of survivin bound to the phosphorylated N- terminal tail of histone H3
4A0N · Baculoviral iap repeat-containing protein 5: “Crystal structure of survivin bound to the phosphorylated N- terminal tail of histone H3”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.47). MolNFT v1 #85061 on…
- PDB
- 4A0N
- Type
- protein
- Length
- 135 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Baculoviral iap repeat-containing protein 5; Histone H3 peptide
- UniProt
- O15392
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Baculoviral iap repeat-containing protein 5 | protein | 131 | 54% helix, 7% strand | O15392 |
| C | Histone H3 peptide | protein | 4 | 0% helix, 50% strand | — |
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 | 100 | 0.47 | 0.80 | 16 | empty |
Interfaces
1 interface between chains.
- A–C · 350 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 4A0N · Crystal structure of Survivin bound to the phosphorylated N-terminal tail of histone H3 · 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 0.95
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 4A0N · PDBe 4A0N · UniProt O15392
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