Research workbench
Crystal structure of human survivin bound to histone H3 phosphorylated on threonine-3 (C2 space group).
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
- 3UED
- Type
- protein
- Length
- 288 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O15392
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 137 | — | O15392 |
| B, D | — | protein | 6 | — | — |
| C | — | protein | 139 | — | O15392 |
Compared structures
- 3UED · Crystal structure of human Survivin bound to histone H3 phosphorylated on threonine-3 (C2… · 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 C 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 3UED · PDBe 3UED · UniProt O15392
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