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2XCM

COMPLEX OF HSP90 N-TERMINAL, SGT1 CS AND RAR1 CHORD2 DOMAIN

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
C0051087molecular_functionprotein-folding chaperone binding
D0051087molecular_functionprotein-folding chaperone binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ADP A 1211
ChainResidue
AASN39
APHE126
ATHR173
AMET175
AMG1212
AHOH2031
AHOH2078
AHOH2079
AHOH2080
AHOH2081
AHOH2082
AALA43
EHIS188
AASP81
AMET86
AASN94
ALEU95
AGLY123
AVAL124
AGLY125

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 1212
ChainResidue
AASN39
AADP1211
AHOH2016
AHOH2020

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ADP B 1211
ChainResidue
BASN39
BALA43
BASP81
BMET86
BASN94
BGLY123
BVAL124
BGLY125
BPHE126
BTHR173
BMET175
BMG1212
BHOH2013
BHOH2027
BHOH2069
BHOH2070
BHOH2071
FHIS188

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 1212
ChainResidue
BASN39
BADP1211
BHOH2008
FASP189
FHOH2023

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 1222
ChainResidue
ECYS159
ECYS164
ECYS178
EHIS218

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 1223
ChainResidue
EHIS181
ECYS196
ECYS197
ECYS213

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 1222
ChainResidue
FCYS159
FCYS164
FCYS178
FHIS218

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 1223
ChainResidue
FHIS181
FCYS196
FCYS197
FCYS213

Functional Information from PROSITE/UniProt
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE
ChainResidueDetails
ATYR26-GLU35

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:20670895, ECO:0007744|PDB:2XCM
ChainResidueDetails
ECYS159
FCYS164
FCYS178
FHIS181
FCYS196
FCYS197
FCYS213
FHIS218
ECYS164
ECYS178
EHIS181
ECYS196
ECYS197
ECYS213
EHIS218
FCYS159

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PDB entries from 2024-07-10

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