Structure of PDB 8ffw Chain A Binding Site BS02

Receptor Information
>8ffw Chain A (length=630) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESL
TDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSG
TKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWES
SAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFI
GYPITLFVEKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWE
DHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVRRVFIM
DNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCL
ELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASG
DEMVSLKDYCTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYM
IEPIDEYCVQQLKEFEGKTLVSVTKEGLELPEDEEEKKKQEEKKTKFENL
CKIMKDILEKKVEKVVVSNRLVTSPCCIVTSTYGWTANMERIMKAQALRD
NSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVKDLVILLYETAL
LSSGFSLEDPQTHANRIYRMIKLGLGIDED
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain8ffw Chain A Residue 802 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB8ffw Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor
Resolution3.23 Å
Binding residue
(original residue number in PDB)		N51 Q133
Binding residue
(residue number reindexed from 1)		N37 Q119
Annotation score1
Enzymatic activity
Enzyme Commision number 3.6.4.10: non-chaperonin molecular chaperone ATPase.
Gene Ontology
Molecular Function
GO:0002134 UTP binding
GO:0002135 CTP binding
GO:0003723 RNA binding
GO:0003729 mRNA binding
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0005525 GTP binding
GO:0016787 hydrolase activity
GO:0016887 ATP hydrolysis activity
GO:0017098 sulfonylurea receptor binding
GO:0019903 protein phosphatase binding
GO:0023026 MHC class II protein complex binding
GO:0030235 nitric-oxide synthase regulator activity
GO:0030911 TPR domain binding
GO:0031625 ubiquitin protein ligase binding
GO:0032564 dATP binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0042826 histone deacetylase binding
GO:0044183 protein folding chaperone
GO:0044325 transmembrane transporter binding
GO:0048156 tau protein binding
GO:0051020 GTPase binding
GO:0051022 Rho GDP-dissociation inhibitor binding
GO:0051082 unfolded protein binding
GO:0070182 DNA polymerase binding
GO:0097110 scaffold protein binding
GO:0097718 disordered domain specific binding
GO:0140662 ATP-dependent protein folding chaperone
GO:1990782 protein tyrosine kinase binding
Biological Process
GO:0001764 neuron migration
GO:0001934 positive regulation of protein phosphorylation
GO:0002218 activation of innate immune response
GO:0002230 positive regulation of defense response to virus by host
GO:0003009 skeletal muscle contraction
GO:0006457 protein folding
GO:0006839 mitochondrial transport
GO:0006986 response to unfolded protein
GO:0007004 telomere maintenance via telomerase
GO:0009408 response to heat
GO:0009409 response to cold
GO:0009410 response to xenobiotic stimulus
GO:0009651 response to salt stress
GO:0010592 positive regulation of lamellipodium assembly
GO:0010659 cardiac muscle cell apoptotic process
GO:0031396 regulation of protein ubiquitination
GO:0032212 positive regulation of telomere maintenance via telomerase
GO:0032273 positive regulation of protein polymerization
GO:0032728 positive regulation of interferon-beta production
GO:0032880 regulation of protein localization
GO:0034605 cellular response to heat
GO:0042026 protein refolding
GO:0042220 response to cocaine
GO:0042307 positive regulation of protein import into nucleus
GO:0042981 regulation of apoptotic process
GO:0043254 regulation of protein-containing complex assembly
GO:0043335 protein unfolding
GO:0043627 response to estrogen
GO:0045040 protein insertion into mitochondrial outer membrane
GO:0045429 positive regulation of nitric oxide biosynthetic process
GO:0045732 positive regulation of protein catabolic process
GO:0045793 positive regulation of cell size
GO:0046677 response to antibiotic
GO:0050821 protein stabilization
GO:0051131 chaperone-mediated protein complex assembly
GO:0060255 regulation of macromolecule metabolic process
GO:0060452 positive regulation of cardiac muscle contraction
GO:0061684 chaperone-mediated autophagy
GO:0098586 cellular response to virus
GO:0099072 regulation of postsynaptic membrane neurotransmitter receptor levels
GO:1902949 positive regulation of tau-protein kinase activity
GO:1905323 telomerase holoenzyme complex assembly
Cellular Component
GO:0005576 extracellular region
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0009986 cell surface
GO:0016020 membrane
GO:0016323 basolateral plasma membrane
GO:0016324 apical plasma membrane
GO:0031526 brush border membrane
GO:0032991 protein-containing complex
GO:0034774 secretory granule lumen
GO:0036126 sperm flagellum
GO:0042470 melanosome
GO:0043025 neuronal cell body
GO:0043202 lysosomal lumen
GO:0043209 myelin sheath
GO:0044294 dendritic growth cone
GO:0044295 axonal growth cone
GO:0048471 perinuclear region of cytoplasm
GO:0062023 collagen-containing extracellular matrix
GO:0070062 extracellular exosome
GO:0071682 endocytic vesicle lumen
GO:0097226 sperm mitochondrial sheath
GO:0097524 sperm plasma membrane
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:8ffw, PDBe:8ffw, PDBj:8ffw
PDBsum8ffw
PubMed37945740
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

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