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3RLQ

Co-crystal structure of the HSP90 ATP binding domain in complex with 4-(2,4-dichloro-5-methoxyphenyl)-2-methyl-7H-pyrrolo[2,3-d]pyrimidine-5- carbonitrile

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 Residues13
DetailsBINDING SITE FOR RESIDUE 3RQ A 901
ChainResidue
AHOH1
ALEU107
APHE138
ATHR184
AHOH259
ALEU48
AASN51
ASER52
AALA55
AASP93
AILE96
AMET98
AASN106

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 A 902
ChainResidue
AGLU200
AARG201
AHOH244
AHOH250
AHOH298
AHOH316
AHOH322
BGLU62
BLYS69
BHIS154

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 3RQ B 901
ChainResidue
BHOH6
BLEU48
BASN51
BSER52
BALA55
BASP93
BGLY97
BMET98
BASN106
BLEU107
BPHE138
BTHR184
BHOH238
BHOH243
BHOH313

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

246031

PDB entries from 2025-12-10

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