9TPH: Survivin 1-127

Survivin 1-127 in complex with a molecular tweezer-Histone-H3-peptide conjugate. Determined by X-ray diffraction at 2.0 Å resolution. Released 15 Apr 2026.

Method: X-ray diffraction
Resolution: 2.0 Å
Organisms: Homo sapiens, synthetic construct
Chains: 4
Atoms: 2,282
Mol. weight: 32.4 kDa
Ligands: ZN, CA, A1JXR
Released: 15 Apr 2026

Explore 9TPH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9TPH contains 13 α-helices and 8 β-strands across 4 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

Element	Residues	Length	Sheet
α-helix	11-13	3
α-helix	15-20	6
α-helix	35-40	6
β-strand	43-45	3	1
β-strand	55-57	3	1
β-strand	63-65	3	1
α-helix	73-80	8
α-helix	85-88	4
α-helix	93-95	3
α-helix	98-125	28

Chain B: 6 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	11-13	3
α-helix	15-21	7
α-helix	35-40	6
β-strand	43-45	3	2
β-strand	55-57	3	2
β-strand	63-65	3	2
α-helix	73-80	8
α-helix	85-88	4
α-helix	98-122	25

Chains C and D: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	2-3	2	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Baculoviral IAP repeat-containing protein 5	A, B	protein	126	Homo sapiens	O15392 (AlphaFold model)
Histone-H3-peptide conjugated to molecular tweezer	C, D	protein	6	synthetic construct

Sequence of entity 1 (A, B), FASTA

>9TPH_1 Baculoviral IAP repeat-containing protein 5 (chains A, B)
GAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCF
KELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKK
KEFEET

Sequence of entity 2 (C, D), FASTA

>9TPH_2 Histone-H3-peptide conjugated to molecular tweezer (chains C, D)
ARTKXX

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2
CA	Calcium ion	Ca	3
A1JXR	Molecular tweezer (BIRC5)	C46 H37 N3 O8 P2	2

Primary citation

Molecular tweezer-peptide conjugates disrupt the protein-protein interaction between survivin and histone H3 essential in mitosis. Gsell, C., Rebmann, P., Opara, K. et al. Beilstein J Org Chem (2026) 22:557-567. DOI 10.3762/bjoc.22.41 · PubMed

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

2QFA 1.4 Å, Crystal structure of a Survivin-Borealin-INCENP core complex
9TPI 1.8 Å, Survivin 1-122 in complex with a molecular tweezer-Histone-H3-peptide conjugate
6YIF 1.81 Å, Structure of Chromosomal Passenger Complex (CPC) bound to phosphorylated Histone 3…
3UEC 2.18 Å, Crystal structure of human Survivin bound to histone H3 phosphorylated on threonine-3.
2RAW 2.4 Å, Crystal structure of the Borealin-Survivin complex
3UIG 2.4 Å, crystal structure of human Survivin in complex with T3 phosphorylated H3(1-15) peptide
3UIH 2.4 Å, crystal structure of human Survivin in complex with Smac/DIABLO(1-15) peptide
8RUP 2.42 Å, Chromosome Passenger Complex (CPC) localization module in complex with H3.T3p-nucleosome
3UEF 2.45 Å, Crystal structure of human Survivin bound to histone H3 (C2 space group).
7LBO 2.5 Å, Crystal structure of human Survivin bound to histone H3 T3phK4me1 peptide
6YIH 2.55 Å, Structure of Chromosomal Passenger Complex (CPC) bound to phosphorylated Histone 3…
1F3H 2.58 Å, X-ray crystal structure of the human anti-apoptotic protein survivin

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