Structure of PDB 3j2t Chain F

Receptor sequence
>3j2tF (length=1144) Species: 9606 (Homo sapiens) [Search protein sequence]
GITSYVRTVLCEGGVPQRPVVFVTRKKLVNAIQQKLSKLKGEPGWVTIHG
MAGCGKSVLAAEAVRDHSLLEGCFPGGVHWVSVGKQDKSGLLMKLQNLCT
RLDQDESFSQRLPLNIEEAKDRLRILMLRKHPRSLLILDDVWDSWVLKAF
DSQCQILLTTRDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVNMKKA
DLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQLQNKQFKRIR
KSSSYDYEALDEAMSISVEMLREDIKDYYTDLSILQKDVKVPTKVLCILW
DMETEEVEDILQEFVNKSLLFCDRNGKSFRYYLHDLQVDFLTEKNCSQLQ
DLHKKIITQFQRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALM
FSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAVSENFQEFLSLNGHL
LGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQEVDNGMLYLEWINKKNIT
NLSRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIK
AHEDEVLCCAFSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNC
CHFTNSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPD
DKLLASCSADGTLKLWDATSANERKSINVKQFFLNLEDPQEDMEVIVKCC
SWSADGARIMVAAKNKIFLFDIHTSGLLGEIHTGHHSTIQYCDFSPQNHL
AVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQ
TIRLWETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIRRLQLINGRTG
QIDYLTEAQVSCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKK
TVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIFLRGHQETVKDFRLLK
NSRLLSWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTS
ADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIW
NVSNGELLHLCAPLSEEGAATHGGWVTDLCFSPDGKMLISAGGYIKWWNV
VTGESSQTFYTNGTNLKKIHVSPDFKTYVTVDNLGILYILQTLE
3D structure
PDB3j2t Changes in apaf-1 conformation that drive apoptosome assembly.
ChainF
Resolution9.5 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 ATP F F126 V127 R129 G157 C158 G159 K160 S161 V162 P321 S325 F22 V23 R25 G53 C54 G55 K56 S57 V58 P217 S221
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:3j2t, PDBe:3j2t, PDBj:3j2t
PDBsum3j2t
PubMed23521171
UniProtO14727|APAF_HUMAN Apoptotic protease-activating factor 1 (Gene Name=APAF1)

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