Structure of PDB 7dmc Chain A

Receptor sequence
>7dmcA (length=209) Species: 9606 (Homo sapiens) [Search protein sequence]
EVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLT
DPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGT
KAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESS
AGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIG
YPITLFVEK
3D structure
PDB7dmc Dipyridamole interacts with the N-terminal domain of HSP90 and antagonizes the function of the chaperone in multiple cancer cell lines.
ChainA
Resolution2.34 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.4.10: non-chaperonin molecular chaperone ATPase.
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 H9F A N51 A55 D93 M98 L107 A111 G135 F138 T184 V186 N36 A40 D78 M83 L92 A96 G120 F123 T169 V171 BindingDB: IC50=21068.2nM
BS02 MG A I91 T184 I76 T169
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:7dmc, PDBe:7dmc, PDBj:7dmc
PDBsum7dmc
PubMed36513142
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

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