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3RLR

Co-crystal structure of the HSP90 ATP binding domain in complex with 4-(2,4-dichloro-5-methoxyphenyl)-2,6-dimethyl-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 3RR A 901
ChainResidue
AHOH2
ALEU107
APHE138
ATHR184
AHOH277
AHOH4
ALEU48
AASN51
ASER52
AALA55
AASP93
AMET98
AASN106

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 A 902
ChainResidue
AGLU200
AARG201
AHOH261
AHOH307
AHOH308
AHOH322
BGLU62
BLYS69
BHIS154
BHOH315

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 3RR B 901
ChainResidue
BHOH3
BLEU48
BASN51
BSER52
BALA55
BASP93
BASN106
BLEU107
BPHE138
BTHR184
BHOH245

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:
ChainResidueDetails
AASN51
AASP93
APHE138
BASN51
BASP93
BPHE138

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS112
BLYS112

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07901
ChainResidueDetails
ALYS58
ALYS84
BLYS58
BLYS84

224201

PDB entries from 2024-08-28

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