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3O6O

Crystal Structure of the N-terminal domain of an HSP90 from Trypanosoma Brucei, Tb10.26.1080 in the presence of an the inhibitor BIIB021

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 Residues15
DetailsBINDING SITE FOR RESIDUE 94M A 214
ChainResidue
AASN36
ATYR124
AVAL135
ATHR169
AHOH215
AHOH221
AHOH280
ASER37
AALA40
AASP78
AILE81
AGLY82
AMET83
ALEU88
APHE123

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 94M B 214
ChainResidue
BASN36
BALA40
BASP78
BILE81
BGLY82
BMET83
BLEU88
BLEU92
BPHE123
BTYR124
BHOH216
BHOH223
BHOH251
BHOH292
B1PE1300

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 1PE B 1300
ChainResidue
BASN36
BASP39
BALA40
BILE81
B94M214

Functional Information from PROSITE/UniProt
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE
ChainResidueDetails
ATYR23-GLU32

222415

PDB entries from 2024-07-10

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