3UEC: Human Survivin

Crystal structure of human Survivin bound to histone H3 phosphorylated on threonine-3. Determined by X-ray diffraction at 2.18 Å resolution. Released 7 Mar 2012.

Method
X-ray diffraction
Resolution
2.18 Å
Organism
Homo sapiens
Chains
2
Atoms
1,231
Mol. weight
18.17 kDa
Ligands
ZN
Released
7 Mar 2012

Explore 3UEC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3UEC contains 7 α-helices and 4 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 7 helices, 3 β-strands

ElementResiduesLengthSheet
α-helix11-133
α-helix15-206
α-helix35-406
β-strand43-4531
β-strand55-5731
β-strand63-6531
α-helix73-808
α-helix85-884
α-helix93-953
α-helix98-13942
Chain B: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand2-321

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Baculoviral IAP repeat-containing protein 5Aprotein146Homo sapiensO15392 (AlphaFold model)
N-terminal fragment of histone H3Bprotein4
Sequence of entity 1 (A), FASTA
>3UEC_1 Baculoviral IAP repeat-containing protein 5 (chains A)
GSHEMGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQ
CFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKE
TNNKKKEFEETAKKVRRAIEQLAAMD
Sequence of entity 2 (B), FASTA
>3UEC_2 N-TERMINAL FRAGMENT OF HISTONE H3 (chains B)
ARTK

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn1

Water and common crystallization additives (PEG, ACT, 1PE, PG4, EDO) are not listed.

Primary citation

Molecular basis for phosphospecific recognition of histone H3 tails by Survivin paralogues at inner centromeres. Niedzialkowska, E., Wang, F., Porebski, P.J. et al. Mol Biol Cell (2012) 23:1457-1466. DOI 10.1091/mbc.E11-11-0904 · PubMed

Other PDB entries of the same protein (UniProt O15392 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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