Structure of PDB 8gft Chain B Binding Site BS01

Receptor Information

>8gft Chain B (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
GYPITLYLEKEKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTND
WEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVF
IMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKK
CLELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQ
SGDEMTSLSEYVSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFEVV
YMTEPIDEYCVQQLKEFDGKSLVSVTKEGLELPEDEEEKKKMEESKAKFE
NLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTANMERIMKAQAL
RDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVKDLVVLLFET
ALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDE

Ligand information

Ligand ID

ATP

InChI

InChI=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

InChIKey

ZKHQWZAMYRWXGA-KQYNXXCUSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341	Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04	O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0	c1nc(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 3.341	Nc1ncnc2n(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

Formula

C10 H16 N5 O13 P3

Name

ADENOSINE-5'-TRIPHOSPHATE

PDB chain

8gft Chain B Residue 802 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	8gft Hsp90 provides a platform for kinase dephosphorylation by PP5.
Resolution	3.8 Å
Binding residue (original residue number in PDB)	N47 A51 M94 S109 G110 T111 G128 F130 G131 G133 F134 T180
Binding residue (residue number reindexed from 1)	N37 A41 M84 S99 G100 T101 G118 F120 G121 G123 F124 T170
Annotation score	5

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:8gft, PDBe:8gft, PDBj:8gft
PDBsum	8gft
PubMed	37069154
UniProt	P08238\|HS90B_HUMAN Heat shock protein HSP 90-beta (Gene Name=HSP90AB1)

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