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1AMW

ADP BINDING SITE IN THE HSP90 MOLECULAR CHAPERONE

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 Residues19
DetailsBINDING SITE FOR RESIDUE ADP A 300
ChainResidue
AASN92
ALEU93
AGLY121
AVAL122
AGLY123
APHE124
ATHR171
AHOH400
AHOH403
AHOH404
AHOH406
AHOH408
AHOH664
AHOH748
AHOH765
AASN37
AALA41
AASP79
AMET84

site_idS1
Number of Residues5
DetailsADP BINDING SITE.
ChainResidue
AASP79
AASN92
AASN37
APHE124
ALYS98

Functional Information from PROSITE/UniProt
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE
ChainResidueDetails
ATYR24-GLU33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16625188, ECO:0007744|PDB:2CG9
ChainResidueDetails
AGLU33
AMET84
AASN92
ALYS98
ASER99
ATHR171

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16625188, ECO:0000269|PubMed:9230303, ECO:0007744|PDB:1AM1, ECO:0007744|PDB:1AMW, ECO:0007744|PDB:2CG9, ECO:0007744|PDB:2WEP
ChainResidueDetails
AASN37
AASP79
AGLN119

218853

PDB entries from 2024-04-24

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