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4ASF

The structure of modified benzoquinone ansamycins bound to yeast N- terminal Hsp90

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 62U A 1216
ChainResidue
ASER36
ALYS98
AGLU106
AGLY121
AVAL122
AGLY123
APHE124
ATHR171
ALEU173
AHOH2018
AHOH2022
AASN37
AHOH2046
AHOH2057
AASP40
AALA41
ALYS44
AASP79
AMET84
AGLU88
AASN92

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI A 1217
ChainResidue
AGLU28
AHIS197
AHOH2013
AHOH2016

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NI A 1218
ChainResidue
AASP132
AHOH2058
AHOH2069

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NI A 1219
ChainResidue
AASP61
AHOH2033

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

222415

PDB entries from 2024-07-10

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