Structure of PDB 8h77 Chain B

Receptor sequence
>8h77B (length=620) Species: 10090 (Mus musculus) [Search protein sequence]
EVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLT
DPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGT
KAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESS
AGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIG
YPITLYLDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKH
FSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCDELI
PEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFSELA
EDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQSGDEMTSLS
EYVSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEY
CVQQLKEFDGKSLVSVTKEGLELPEDEEEKKKMEESKAKFENLCKLMKEI
LDKKVEKVTISNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYM
MAKKHLEINPDHPIVETLRQKAEADKNDKAVKDLVVLLFETALLSSGFSL
EDPQTHSNRIYRMIKLGLGI
3D structure
PDB8h77 Cryo-EM structure of the cytosolic AhR complex.
ChainB
Resolution3.2 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 ADP B N46 A50 M93 G109 G127 G130 F133 T179 N36 A40 M83 G99 G117 G120 F123 T169
BS02 BEF B E42 N46 G127 E32 N36 G117
Gene Ontology
Molecular Function
GO:0003725 double-stranded RNA binding
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0019887 protein kinase regulator activity
GO:0019900 kinase binding
GO:0019901 protein kinase binding
GO:0030235 nitric-oxide synthase regulator activity
GO:0030911 TPR domain binding
GO:0031072 heat shock protein binding
GO:0031625 ubiquitin protein ligase binding
GO:0042277 peptide binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0042826 histone deacetylase binding
GO:0043008 ATP-dependent protein binding
GO:0044183 protein folding chaperone
GO:0046983 protein dimerization activity
GO:0048156 tau protein binding
GO:0051082 unfolded protein binding
GO:0070182 DNA polymerase binding
GO:0097718 disordered domain specific binding
GO:0140662 ATP-dependent protein folding chaperone
GO:0141069 receptor ligand inhibitor activity
GO:1990226 histone methyltransferase binding
Biological Process
GO:0001890 placenta development
GO:0006457 protein folding
GO:0007004 telomere maintenance via telomerase
GO:0019062 virion attachment to host cell
GO:0030511 positive regulation of transforming growth factor beta receptor signaling pathway
GO:0031396 regulation of protein ubiquitination
GO:0032435 negative regulation of proteasomal ubiquitin-dependent protein catabolic process
GO:0032880 regulation of protein localization
GO:0034605 cellular response to heat
GO:0043066 negative regulation of apoptotic process
GO:0045429 positive regulation of nitric oxide biosynthetic process
GO:0045597 positive regulation of cell differentiation
GO:0051131 chaperone-mediated protein complex assembly
GO:0051726 regulation of cell cycle
GO:0061077 chaperone-mediated protein folding
GO:0071353 cellular response to interleukin-4
GO:0097435 supramolecular fiber organization
GO:1901799 negative regulation of proteasomal protein catabolic process
GO:1905323 telomerase holoenzyme complex assembly
GO:2000010 positive regulation of protein localization to cell surface
Cellular Component
GO:0005576 extracellular region
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0008180 COP9 signalosome
GO:0032991 protein-containing complex
GO:0034751 aryl hydrocarbon receptor complex
GO:0042470 melanosome
GO:0043025 neuronal cell body
GO:0044294 dendritic growth cone
GO:0044295 axonal growth cone
GO:0048471 perinuclear region of cytoplasm
GO:0101031 protein folding chaperone complex
GO:0120293 dynein axonemal particle
GO:1990565 HSP90-CDC37 chaperone complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8h77, PDBe:8h77, PDBj:8h77
PDBsum8h77
PubMed36649707
UniProtP11499|HS90B_MOUSE Heat shock protein HSP 90-beta (Gene Name=Hsp90ab1)

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