1CY5: Apaf-1 card

Crystal structure of the apaf-1 card. Determined by X-ray diffraction at 1.3 Å resolution. Released 13 Sept 1999.

Method
X-ray diffraction
Resolution
1.3 Å
Organism
Homo sapiens
Chains
1
Atoms
861
Mol. weight
11.5 kDa
Ligands
ZN
Released
13 Sept 1999

Explore 1CY5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1CY5 contains 8 α-helices and 0 β-strands across 1 chain. 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: 8 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix3-119
α-helix13-197
α-helix22-3211
α-helix37-448
α-helix49-6113
α-helix65-7713
α-helix81-877
α-helix88-903

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein (apoptotic protease activating factor 1)Aprotein97Homo sapiensO14727 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1CY5_1 PROTEIN (APOPTOTIC PROTEASE ACTIVATING FACTOR 1) (chains A)
MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMI
LKKDNDSYVSFYNALLHEGYKDLAALLHDGIPVVSSS

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn5

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

Primary citation

Crystal structure of Apaf-1 caspase recruitment domain: an alpha-helical Greek key fold for apoptotic signaling. Vaughn, D.E., Rodriguez, J., Lazebnik, Y. et al. J Mol Biol (1999) 293:439-447. DOI 10.1006/jmbi.1999.3177 · PubMed

Other PDB entries of the same protein (UniProt O14727 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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