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5LR1

CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH A003498614A.

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
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue 72Y A 4000
ChainResidue
AASN51
ATRP162
ATHR184
AHOH4179
AHOH4196
AHOH4281
AALA55
AASP93
AILE96
AGLY97
AMET98
ALEU107
APHE138
ATYR139

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 Residues3
DetailsBINDING:
ChainResidueDetails
APHE138
AASN51
AASP93

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS112

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07901
ChainResidueDetails
ALYS84
ALYS58

219869

PDB entries from 2024-05-15

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