Structure of PDB 5juy Chain B

Receptor sequence

>5juyB (length=1234) Species: 9606 (Homo sapiens) [Search protein sequence]

MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQ
QRAAMLIKMILKKDNDSYVSFYNALLHEGYKDLAALLHDGIPVVSGITSY
VRTVLCEGGVPQRPVVFVTRKKLVNAIQQKLSKLKGEPGWVTIHGMAGCG
KSVLAAEAVRDHSLLEGCFPGGVHWVSVGKQDKSGLLMKLQNLCTRLDQD
ESFSQRLPLNIEEAKDRLRILMLRKHPRSLLILDDVWDSWVLKAFDSQCQ
ILLTTRDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVNMKKADLPEQ
AHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQLQNKQFKRIRKSSSY
DYEALDEAMSISVEMLREDIKDYYTDLSILQKDVKVPTKVLCILWDMETE
EVEDILQEFVNKSLLFCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKK
IITQFQRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALMFSLDW
IKAKTELVGPAHLIHEFVEYRHILDEKDCAVSENFQEFLSLNGHLLGRQP
FPNIVQLGLCEPETSEVYQQAKLQAKQEVDNGMLYLEWINKKNITNLSRL
VVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDE
VLCCAFSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNCCHFTN
SSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLA
SCSADGTLKLWDATSANERKSINVKQFFLNEDMEVIVKCCSWSADGARIM
VAAKNKIFLFDIHTSGLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCV
ELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWETKKV
CKNSAVMLKQEVDVVFQENEVMVLAVDHIRRLQLINGRTGQIDYLTEAQV
SCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTAD
EKTLISSSDDAEIQVWNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFD
GTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSF
DLLLPLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHL
CAPLSEEGAATHGGWVTDLCFSPDGKMLISAGGYIKWWNVVTGESSQTFY
TNGTNLKKIHVSPDFKTYVTVDNLGILYILQTLE

3D structure

PDB

5juy A near atomic structure of the active human apoptosome.

Chain

Resolution

4.1 Å

3D
structure

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Enzymatic activity

Enzyme Commision number

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	DTP	B	F126 C158 G159 K160 S161 R265 P321	F117 C149 G150 K151 S152 R256 P312

Gene Ontology

	Molecular Function
GO:0000166	nucleotide binding
GO:0005515	protein binding
GO:0005524	ATP binding
GO:0008656	cysteine-type endopeptidase activator activity involved in apoptotic process
GO:0031072	heat shock protein binding
GO:0042802	identical protein binding
GO:0043531	ADP binding

	Biological Process
GO:0001666	response to hypoxia
GO:0001822	kidney development
GO:0001843	neural tube closure
GO:0006915	apoptotic process
GO:0006919	activation of cysteine-type endopeptidase activity involved in apoptotic process
GO:0007399	nervous system development
GO:0007420	brain development
GO:0007584	response to nutrient
GO:0008635	activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c
GO:0010659	cardiac muscle cell apoptotic process
GO:0030154	cell differentiation
GO:0030900	forebrain development
GO:0042981	regulation of apoptotic process
GO:0043065	positive regulation of apoptotic process
GO:0051402	neuron apoptotic process
GO:0070059	intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress
GO:0071560	cellular response to transforming growth factor beta stimulus
GO:0072432	response to G1 DNA damage checkpoint signaling
GO:0097190	apoptotic signaling pathway
GO:0097193	intrinsic apoptotic signaling pathway
GO:1902510	regulation of apoptotic DNA fragmentation
GO:2001235	positive regulation of apoptotic signaling pathway

	Cellular Component
GO:0005576	extracellular region
GO:0005634	nucleus
GO:0005737	cytoplasm
GO:0005829	cytosol
GO:0032991	protein-containing complex
GO:0034774	secretory granule lumen
GO:0043293	apoptosome
GO:0070062	extracellular exosome
GO:1904813	ficolin-1-rich granule lumen

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:5juy, PDBe:5juy, PDBj:5juy
PDBsum	5juy
PubMed	27697150
UniProt	O14727\|APAF_HUMAN Apoptotic protease-activating factor 1 (Gene Name=APAF1)

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