Structure of PDB 7zr0 Chain A Binding Site BS01

Receptor Information
>7zr0 Chain A (length=633) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESL
TDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSG
TKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWES
SAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFI
GYPITLYLEKEREKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLT
NDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRR
VFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIV
KKCLELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHT
SQSGDEMTSLSEYVSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFE
VVYMTEPIDEYCVQQLKEFDGKSLVSVTKEGLELPEDEEEKKKMEESKAK
FENLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTANMERIMKAQ
ALRDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVKDLVVLLF
ETALLSSGFSLEDPQTHSNRIYRMIKLGLGIDE
Ligand information
Ligand IDATP
InChIInChI=1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyZKHQWZAMYRWXGA-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=O)(O)O[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@](O)(=O)O[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
FormulaC10 H16 N5 O13 P3
NameADENOSINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL14249
DrugBankDB00171
ZINCZINC000004261765
PDB chain7zr0 Chain A Residue 801 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB7zr0 HSP90-CDC37-PP5 forms a structural platform for kinase dephosphorylation.
Resolution3.4 Å
Binding residue
(original residue number in PDB)		N46 N101 S108 G109
Binding residue
(residue number reindexed from 1)		N37 N92 S99 G100
Annotation score5
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0003723 RNA binding
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:0023026 MHC class II protein complex 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:0045296 cadherin binding
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:0006986 response to unfolded protein
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:0050821 protein stabilization
GO:0051131 chaperone-mediated protein complex assembly
GO:0051726 regulation of cell cycle
GO:0060255 regulation of macromolecule metabolic process
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:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0008180 COP9 signalosome
GO:0009986 cell surface
GO:0016020 membrane
GO:0032991 protein-containing complex
GO:0034751 aryl hydrocarbon receptor complex
GO:0034774 secretory granule lumen
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:0070062 extracellular exosome
GO:0101031 protein folding chaperone complex
GO:0120293 dynein axonemal particle
GO:1904813 ficolin-1-rich granule lumen
GO:1990565 HSP90-CDC37 chaperone complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:7zr0, PDBe:7zr0, PDBj:7zr0
PDBsum7zr0
PubMed36446791
UniProtP08238|HS90B_HUMAN Heat shock protein HSP 90-beta (Gene Name=HSP90AB1)

[Back to BioLiP]