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6LTI

HSP90 in complex with NVP-AUY922

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 Residues21
Detailsbinding site for residue 2GJ A 301
ChainResidue
ALEU48
ALEU107
ATHR109
APHE138
ATHR184
AVAL186
AHOH412
AHOH429
AHOH438
AHOH444
AHOH453
AASN51
AHOH455
AHOH481
AALA55
ALYS58
AASP93
AILE96
AGLY97
AMET98
AASP102

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 302
ChainResidue
AHOH428
AHOH428
AHOH551
AHOH551
AHOH559
AHOH559

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

222926

PDB entries from 2024-07-24

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