1F3H: Human anti-apoptotic protein survivin

X-ray crystal structure of the human anti-apoptotic protein survivin. Determined by X-ray diffraction at 2.58 Å resolution. Released 6 Dec 2000.

Method
X-ray diffraction
Resolution
2.58 Å
Organism
Homo sapiens
Chains
2
Atoms
2,320
Mol. weight
33.28 kDa
Ligands
ZN
Released
6 Dec 2000

Explore 1F3H in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1F3H contains 13 α-helices and 10 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, 6 β-strands

ElementResiduesLengthSheet
α-helix8-136
α-helix15-195
α-helix35-395
β-strand43-4531
β-strand4812
β-strand5112
β-strand55-5731
β-strand63-6421
α-helix73-808
α-helix86-883
α-helix93-953
β-strand9713
α-helix98-13639
Chain B: 6 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix11-133
α-helix15-206
β-strand43-4534
β-strand55-5734
β-strand63-6424
α-helix73-786
α-helix85-884
α-helix93-953
β-strand9713
α-helix98-13639

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
SurvivinA, Bprotein142Homo sapiensO15392 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1F3H_1 SURVIVIN (chains A, B)
MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDMAQCFFC
FKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNK
KKEFEETAKKVRRAIEQLAAMD

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

Water and common crystallization additives (SO4) are not listed.

Primary citation

Structure of the human anti-apoptotic protein survivin reveals a dimeric arrangement. Verdecia, M.A., Huang, H., Dutil, E. et al. Nat Struct Biol (2000) 7:602-608. DOI 10.1038/77929 · PubMed

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

Browse structure collections

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