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3VHD

Hsp90 alpha N-terminal domain in complex with a macrocyclic inhibitor, CH5164840

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0006457biological_processprotein folding
A0016887molecular_functionATP hydrolysis activity
A0051082molecular_functionunfolded protein binding
A0140662molecular_functionATP-dependent protein folding chaperone
B0005524molecular_functionATP binding
B0006457biological_processprotein folding
B0016887molecular_functionATP hydrolysis activity
B0051082molecular_functionunfolded protein binding
B0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE VHE A 1
ChainResidue
AHOH5
APHE138
ATHR184
AHOH240
AHOH260
AHOH399
AHOH522
BGLU120
AHOH6
ASER52
AALA55
ALYS58
AASP93
AGLY97
AASN106
ALEU107

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE VHE B 1
ChainResidue
AGLU120
BHOH4
BHOH7
BSER52
BALA55
BLYS58
BASP93
BGLY97
BMET98
BASN106
BLEU107
BPHE138
BTHR184
BHOH237
BHOH277
BHOH355

Functional Information from PROSITE/UniProt
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE
ChainResidueDetails
ATYR38-GLU47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07901","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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