{"context":{"query":">>uniprot>>pdb","source_dataset":"uniprot","target_dataset":"pdb"},"stats":{"queried":1,"total":36,"mapped":1},"pagination":{"has_next":false},"schema":"id|title|method|resolution|source_organism|chain_count|header","mappings":[{"input":"Q14790","source":"Q14790|Caspase-8","targets":["1F9E|CASPASE-8 SPECIFICITY PROBED AT SUBSITE S4: CRYSTAL STRUCTURE OF THE CASPASE-8-Z-DEVD-CHO|X-RAY DIFFRACTION|2.9|Homo sapiens; SYNTHETIC CONSTRUCT|0|HYDROLASE/HYDROLASE INHIBITOR","1I4E|CRYSTAL STRUCTURE OF THE CASPASE-8/P35 COMPLEX|X-RAY DIFFRACTION|3|Autographa californica nucleopolyhedrovirus; Homo sapiens|0|APOPTOSIS/HYDROLASE","1QDU|CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TRIPEPTIDE KETONE INHIBITOR ZEVD-DCBMK|X-RAY DIFFRACTION|2.8|Homo sapiens; SYNTHETIC CONSTRUCT|0|HYDROLASE/HYDROLASE INHIBITOR","1QTN|CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TETRAPEPTIDE INHIBITOR ACE-IETD-ALDEHYDE|X-RAY DIFFRACTION|1.2|Homo sapiens; SYNTHETIC CONSTRUCT|0|HYDROLASE/HYDROLASE INHIBITOR","2C2Z|Crystal structure of caspase-8 in complex with aza-peptide Michael acceptor inhibitor|X-RAY DIFFRACTION|1.95|HOMO SAPIENS; SYNTHETIC CONSTRUCT|0|HYDROLASE/HYDROLASE INHIBITOR","2FUN|alternative p35-caspase-8 complex|X-RAY DIFFRACTION|3|Autographa californica nucleopolyhedrovirus; Homo sapiens|0|APOPTOSIS/HYDROLASE","2K7Z|Solution Structure of the Catalytic Domain of Procaspase-8|SOLUTION NMR||Homo sapiens|0|HYDROLASE","2Y1L|Caspase-8 in Complex with DARPin-8.4|X-RAY DIFFRACTION|1.8|; Homo sapiens; SYNTHETIC CONSTRUCT; SYNTHETIC CONSTRUCT|0|HYDROLASE/INHIBITOR","3H11|Zymogen caspase-8:c-FLIPL protease domain complex|X-RAY DIFFRACTION|1.9|Homo sapiens; SYNTHETIC CONSTRUCT|0|APOPTOSIS","3KJN|Caspase 8 bound to a covalent inhibitor|X-RAY DIFFRACTION|1.8|Homo sapiens|0|HYDROLASE/HYDROLASE INHIBITOR","3KJQ|Caspase 8 with covalent inhibitor|X-RAY DIFFRACTION|1.8|Homo sapiens|0|HYDROLASE","4JJ7|Caspase-3 specific unnatural amino acid-based peptides|X-RAY DIFFRACTION|1.178|Homo sapiens; SYNTHETIC CONSTRUCT|0|HYDROLASE/HYDROLASE INHIBITOR","4PRZ|Caspase-8 specific unnatural amino acid peptides|X-RAY DIFFRACTION|2.123|Homo sapiens; SYNTHETIC CONSTRUCT|0|HYDROLASE/HYDROLASE INHIBITOR","4PS1|Caspase-8 specific unnatural amino acid peptides|X-RAY DIFFRACTION|1.731|Homo sapiens; SYNTHETIC CONSTRUCT|0|HYDROLASE/HYDROLASE INHIBITOR","4ZBW|Crystal structure of death effector domain of Caspase8 in Homo Sapiens|X-RAY DIFFRACTION|2.2|Homo sapiens|0|HYDROLASE","5H31|Structural basis for dimerization of the death effector domains of Caspase-8|X-RAY DIFFRACTION|3.16954|Homo sapiens|0|HYDROLASE","5H33|Structural basis for dimerization of the death effector domains of Caspase-8|X-RAY DIFFRACTION|3.60014|Homo sapiens|0|HYDROLASE","5JQE|Crystal structure of caspase8 tDED|X-RAY DIFFRACTION|3.157|Escherichia coli, Homo sapiens|0|HYDROLASE","5L08|Cryo-EM structure of Casp-8 tDED filament|ELECTRON MICROSCOPY|4.6|Homo sapiens|0|APOPTOSIS","6AGW|Pro-domain of Caspase-8|X-RAY DIFFRACTION|2.093|Homo sapiens|0|HYDROLASE","6PX9|Crystal structure of procaspase-8 in complex with covalent small molecule inhibitor 63-R|X-RAY DIFFRACTION|2.88|Homo sapiens|0|HYDROLASE/HYDROLASE INHIBITOR","6X8H|Caspase-8 in complex with AOMK inhibitor, Ac-DW3-KE, forms tetrahedral adduct|X-RAY DIFFRACTION|1.48|Homo sapiens; SYNTHETIC CONSTRUCT|0|HYDROLASE/HYDROLASE INHIBITOR","7DEE|Structural Basis of the regulation of DISC Assembly by the interaction of c-FLIPs with Procaspase-8|SOLUTION NMR||Homo sapiens|0|APOPTOSIS","7LVJ|CASP8 isoform G DED domain|X-RAY DIFFRACTION|1.5|Homo sapiens|0|HYDROLASE","7LVM|CASP8 isoform B DED domain|X-RAY DIFFRACTION|1.47|Homo sapiens|0|HYDROLASE","8YBX|Structure of the FADD/Caspase-8/cFLIP death effector domain assembly|ELECTRON MICROSCOPY|3.68|Homo sapiens|0|APOPTOSIS","8YD7|Structure of FADD/Caspase-8/cFLIP death effector domain assembly|X-RAY DIFFRACTION|3.32|Homo sapiens|0|APOPTOSIS","8YD8|Structure of FADD/Caspase-8/cFLIP death effector domain assembly|X-RAY DIFFRACTION|3.11|Homo sapiens|0|APOPTOSIS","8YM4|Structure of Caspase-8/cFLIP death effector domain assembly|X-RAY DIFFRACTION|2.34|Homo sapiens|0|APOPTOSIS","8YM5|Structure of Caspase-8/cFLIP death effector domain assembly|X-RAY DIFFRACTION|2.09|Homo sapiens|0|APOPTOSIS","8YM6|Structure of Caspase-8/cFLIP death effector domain assembly|X-RAY DIFFRACTION|3.3|Homo sapiens|0|APOPTOSIS","8YNI|Structure of the FADD/Caspase-8/cFLIP death effector domain assembly|ELECTRON MICROSCOPY|3.66|Homo sapiens|0|APOPTOSIS","8YNK|Structure of the Caspase-8/cFLIP death effector domain assembly|ELECTRON MICROSCOPY|3.62|Homo sapiens|0|APOPTOSIS","8YNL|Structure of the Caspase-8/cFLIP death effector domain assembly|ELECTRON MICROSCOPY|3.55|Homo sapiens|0|APOPTOSIS","8YNM|Structure of the Caspase-8/cFLIP death effector domain assembly|ELECTRON MICROSCOPY|3.49|Homo sapiens|0|APOPTOSIS","8YNN|Structure of the Caspase-8/cFLIP death effector domain assembly|ELECTRON MICROSCOPY|3.97|Homo sapiens|0|APOPTOSIS"]}]}