Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T18477 Target Info
Target Name Heat shock protein 90 alpha (HSP90A)
Synonyms Renal carcinoma antigen NY-REN-38; Lipopolysaccharide-associated protein 2; LPS-associated protein 2; LAP-2; Heat shock protein HSP 90-alpha; Heat shock 86 kDa; HSPCA; HSPC1; HSP90A; HSP86; HSP 86
Target Type Successful Target
Gene Name HSP90AA1
Biochemical Class Heat shock protein
UniProt ID
HS90A_HUMAN
Ligand General Information  Top
Ligand Name Adenosine triphosphate Ligand Info
Canonical SMILES C1=NC(=C2C(=N1)N(C=N2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N
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
PubChem Compound ID 5957
Drug Binding Sites of Target  Top
PDB ID: 7KRJ      The GR-Maturation Complex: Glucocorticoid Receptor in complex with Hsp90 and co-chaperone p23
Method Electron microscopy Resolution 2.56 Å Mutation Yes [1]
PDB Sequence
EEVETFAFQA
24
EIAQLMSLII
34
NTFYSNKEIF
44
LRELISNSSD
54
ALDKIRYESL
64

TDPSKLDSGK
74
ELHINLIPNK
84
QDRTLTIVDT
94
GIGMTKADLI
104
NNLGTIAKSG
114

TKAFMEALQA
124
GADISMIGQF
134
GVGFYSAYLV
144
AEKVTVITKH
154
NDDEQYAWES
164

SAGGSFTVRT
174
DTGEPMGRGT
184
KVILHLKEDQ
194
TEYLEERRIK
204
EIVKKHSQFI
214

GYPITLFVEK
224
EKYIDQEELN
291
KTKPIWTRNP
301
DDITNEEYGE
311
FYKSLTNDWE
321

DHLAVKHFSV
331
EGQLEFRALL
341
FVPRRAPFDL
351
FENRKKKNNI
361
KLYVRRVFIM
371

DNCEELIPEY
381
LNFIRGVVDS
391
EDLPLNISRE
401
MLQQSKILKV
411
IRKNLVKKCL
421

ELFTELAEDK
431
ENYKKFYEQF
441
SKNIKLGIHE
451
DSQNRKKLSE
461
LLRYYTSASG
471

DEMVSLKDYC
481
TRMKENQKHI
491
YYITGETKDQ
501
VANSAFVERL
511
RKHGLEVIYM
521

IEPIDEYCVQ
531
QLKEFEGKTL
541
VSVTKEGLEL
551
PEDEEEKKKQ
561
EEKKTKFENL
571

CKIMKDILEK
581
KVEKVVVSNR
591
LVTSPCCIVT
601
STYGWTANME
611
RIMKAQALRD
621

NSTMGYMAAK
631
KHLEINPDHS
641
IIETLRQKAE
651
ADKNDKSVKD
661
LVILLYETAL
671

LSSGFSLEDP
681
QTHANRIYRM
691
IKLGLGI
Residue
Distance (Å)
TYR38
4.541
GLU47
3.533
LEU48
4.802
ASN51
2.625
SER52
3.011
ASP54
4.649
ALA55
2.785
LYS58
2.973
ASP93
3.363
ILE96
3.154
GLY97
2.964
MET98
2.326
ASP102
4.825
ASN106
2.327
LEU107
3.231
LYS112
3.179
Residue
Distance (Å)
SER113
2.466
GLY114
2.003
THR115
2.069
LYS116
4.214
ILE131
3.948
GLY132
2.530
GLN133
2.095
PHE134
2.183
GLY135
2.053
VAL136
3.068
GLY137
2.548
PHE138
1.868
TYR139
4.267
THR184
2.166
VAL186
3.769
ARG400
3.203
PDB ID: 3T0Z      Hsp90 N-terminal domain bound to ATP
Method X-ray diffraction Resolution 2.19 Å Mutation No [2]
PDB Sequence
PMEEEEVETF
20
AFQAEIAQLM
30
SLIINTFYSN
40
KEIFLRELIS
50
NSSDALDKIR
60

YESLTDPSKL
70
DSGKELHINL
80
IPNKQDRTLT
90
IVDTGIGMTK
100
ADLINNLGTI
110

AKSGTKAFME
120
ALQAGADISM
130
IGQFGVGFYS
140
AYLVAEKVTV
150
ITKHNDDEQY
160

AWESSAGGSF
170
TVRTDTGEPM
180
GRGTKVILHL
190
KEDQTEYLEE
200
RRIKEIVKKH
210

SQFIGYPITL
220
FVE
Residue
Distance (Å)
GLU47
3.861
ASN51
2.903
SER52
3.966
ASP54
4.205
ALA55
3.286
LYS58
4.937
ASP93
2.948
ILE96
4.203
GLY97
4.196
MET98
3.505
ASN106
3.710
LEU107
3.794
Residue
Distance (Å)
LYS112
4.161
ILE131
3.724
GLY132
2.423
GLN133
4.347
PHE134
3.891
GLY135
2.649
VAL136
2.901
GLY137
3.179
PHE138
2.944
TYR139
4.513
THR184
3.290
References  Top
REF 1 Structure of Hsp90-p23-GR reveals the Hsp90 client-remodelling mechanism. Nature. 2022 Jan;601(7893):465-469.
REF 2 Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90. Acta Biochim Biophys Sin (Shanghai). 2012 Apr;44(4):300-6.

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