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6LR9

HSP90 in complex with Debio0932

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 Residues13
Detailsbinding site for residue EOR A 301
ChainResidue
AASN51
AGOL302
AHOH415
AHOH463
AHOH489
AALA55
AASP93
AMET98
ALEU107
APHE138
ATYR139
ATRP162
ATHR184

site_idAC2
Number of Residues10
Detailsbinding site for residue GOL A 302
ChainResidue
APHE22
AASP102
ALEU103
AILE104
AASN105
ALEU107
AGLY108
ATYR139
ATRP162
AEOR301

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
AASN51
AASP93
APHE138

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
ALYS58
ALYS84

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:2492519, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER231

222415

PDB entries from 2024-07-10

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