MolNFT v1 · #81165 · protein
Crystal structure of human survivin in complex with H3(1-10) peptide
3UII · Baculoviral iap repeat-containing protein 5: “Crystal structure of human survivin in complex with H3(1-10) peptide”. X-ray diffraction, 1 ligand (ZN), 3 pockets (best druggability 0.67). MolNFT v1 #81165 on GenesisL1: 3D structure…
- PDB
- 3UII
- Type
- protein
- Length
- 278 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Baculoviral iap repeat-containing protein 5; Histone H3(1-10) peptide
- UniProt
- O15392
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Baculoviral iap repeat-containing protein 5 | protein | 135 | 50% helix, 7% strand | O15392 |
| P, Q | Histone H3(1-10) peptide | protein | 4 | 0% helix, 50% strand | — |
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 | 93 | 0.67 | 0.91 | 20 | empty |
| 2 | 125 | 0.52 | 0.80 | 22 | empty |
| 3 | 108 | 0.48 | 0.80 | 21 | empty |
Interfaces
3 interfaces between chains.
- A–B · 585 Ų buried · 5 hydrogen bonds · protein-protein
- A–P · 381 Ų buried · 11 hydrogen bonds · protein-protein
- B–Q · 374 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 3UII · crystal structure of human Survivin in complex with H3(1-10) peptide · 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 0.98
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 3UII · PDBe 3UII · UniProt O15392
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