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7RY1

human Hsp90_MC domain structure

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
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG400
BARG400
CARG400

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P07901
ChainResidueDetails
ATYR313
ATYR492
BTYR313
BTYR492
CTYR313
CTYR492

site_idSWS_FT_FI3
Number of Residues12
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS443
CLYS458
CLYS489
CLYS585
ALYS458
ALYS489
ALYS585
BLYS443
BLYS458
BLYS489
BLYS585
CLYS443

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P82995
ChainResidueDetails
ASER453
BSER453
CSER453

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER476
ASER641
BSER476
BSER641
CSER476
CSER641

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:15937123
ChainResidueDetails
ACYS598
BCYS598
CCYS598

226707

PDB entries from 2024-10-30

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