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3WHA

Hsp90 alpha N-terminal domain in complex with a tricyclic inhibitor

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 Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
AASP54
AASP57
ALYS112
ASER113
AGLY114
AHOH559
AHOH567
AHOH571

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE WHA A 302
ChainResidue
AASP54
AALA55
ALYS58
AASP93
AILE96
AGLY97
AMET98
AASN106
ALEU107
AGLY135
APHE138
ATYR139
ATHR184
AHOH401
AHOH403
AHOH408
AHOH410
AHOH414
AHOH670
ASER52

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE WHA B 301
ChainResidue
BALA55
BASP93
BILE96
BGLY97
BMET98
BASN106
BLEU107
BPHE138
BTYR139
BTHR184
BHOH401
BHOH403
BHOH404
BHOH409
BHOH417
BHOH630
BHOH670

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 302
ChainResidue
BHOH699
BHOH699
BHOH700
BHOH700
BHOH701
BHOH701

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

site_idSWS_FT_FI4
Number of Residues2
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
BSER231

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PDB entries from 2024-07-31

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