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3B24

Hsp90 alpha N-terminal domain in complex with an aminotriazine fragment molecule

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 Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1
ChainResidue
AHOH362
AHOH362
AHOH428
AHOH428
AHOH457
AHOH457

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE B2J A 237
ChainResidue
ALYS58
AASP93
AGLY97
AMET98
ALEU107
ATHR184
AHOH247
AHOH253
AHOH306
AHOH469
AASN51
ASER52
AALA55

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE B2J B 2
ChainResidue
BHOH3
BHOH4
BHOH7
BSER52
BALA55
BASP93
BGLY97
BMET98
BTHR184
BHOH489

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

239492

PDB entries from 2025-07-30

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