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7ULJ

Hsp90b N-terminal domain in complex with 42C

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
C0005524molecular_functionATP binding
C0006457biological_processprotein folding
C0016887molecular_functionATP hydrolysis activity
C0051082molecular_functionunfolded protein binding
C0140662molecular_functionATP-dependent protein folding chaperone
D0005524molecular_functionATP binding
D0006457biological_processprotein folding
D0016887molecular_functionATP hydrolysis activity
D0051082molecular_functionunfolded protein binding
D0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PROSITE/UniProt
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE
ChainResidueDetails
ATYR33-GLU42

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASN46
DASN46
DLYS107
DPHE133
ALYS107
APHE133
BASN46
BLYS107
BPHE133
CASN46
CLYS107
CPHE133

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AASP88
BASP88
CASP88
DASP88

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Cleaved under oxidative stress => ECO:0000269|PubMed:22848402
ChainResidueDetails
AILE126
BILE126
CILE126
DILE126

221716

PDB entries from 2024-06-26

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