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4AWO

Complex of HSP90 ATPase domain with tropane derived inhibitors

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 Residues19
DetailsBINDING SITE FOR RESIDUE 99B A 1225
ChainResidue
AALA21
AILE104
AASN105
AASN106
ALEU107
APHE138
ATYR139
ATRP162
APHE170
AHOH2029
AHOH2080
APHE22
AGLN23
AASN51
ASER52
AALA55
AASP93
AMET98
ALEU103

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 99B B 1225
ChainResidue
ALYS224
BALA21
BPHE22
BGLN23
BASN51
BSER52
BALA55
BASP93
BMET98
BLEU103
BILE104
BASN105
BASN106
BLEU107
BILE110
BPHE138
BTYR139
BTRP162
BPHE170
BHOH2020
BHOH2057

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

223166

PDB entries from 2024-07-31

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