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2CG9

Crystal structure of an Hsp90-Sba1 closed chaperone complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000492biological_processbox C/D snoRNP assembly
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006457biological_processprotein folding
A0006458biological_process'de novo' protein folding
A0006626biological_processprotein targeting to mitochondrion
A0006970biological_processresponse to osmotic stress
A0016887molecular_functionATP hydrolysis activity
A0032204biological_processregulation of telomere maintenance
A0032212biological_processpositive regulation of telomere maintenance via telomerase
A0032991cellular_componentprotein-containing complex
A0034605biological_processcellular response to heat
A0042026biological_processprotein refolding
A0042802molecular_functionidentical protein binding
A0043248biological_processproteasome assembly
A0048471cellular_componentperinuclear region of cytoplasm
A0050821biological_processprotein stabilization
A0051082molecular_functionunfolded protein binding
A0051604biological_processprotein maturation
A0070482biological_processresponse to oxygen levels
A0140662molecular_functionATP-dependent protein folding chaperone
B0000492biological_processbox C/D snoRNP assembly
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006457biological_processprotein folding
B0006458biological_process'de novo' protein folding
B0006626biological_processprotein targeting to mitochondrion
B0006970biological_processresponse to osmotic stress
B0016887molecular_functionATP hydrolysis activity
B0032204biological_processregulation of telomere maintenance
B0032212biological_processpositive regulation of telomere maintenance via telomerase
B0032991cellular_componentprotein-containing complex
B0034605biological_processcellular response to heat
B0042026biological_processprotein refolding
B0042802molecular_functionidentical protein binding
B0043248biological_processproteasome assembly
B0048471cellular_componentperinuclear region of cytoplasm
B0050821biological_processprotein stabilization
B0051082molecular_functionunfolded protein binding
B0051604biological_processprotein maturation
B0070482biological_processresponse to oxygen levels
B0140662molecular_functionATP-dependent protein folding chaperone
X0051879molecular_functionHsp90 protein binding
Y0051879molecular_functionHsp90 protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP A1678
ChainResidue
AGLU33
AGLY118
AGLN119
AGLY121
AVAL122
AGLY123
APHE124
ATHR171
AARG380
AASN37
AALA38
AALA41
AASP79
AMET84
AASN92
ASER99
AGLY100

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP B1678
ChainResidue
BGLU33
BASN37
BASP40
BALA41
BASP79
BMET84
BASN92
BSER99
BGLY100
BGLY118
BGLN119
BPHE120
BGLY121
BVAL122
BGLY123
BPHE124
BTHR171
BARG380

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 Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:9298649
ChainResidueDetails
XASP3
BASN92
BLYS98
BSER99
BTHR171
BARG380
YASP3
AASN92
ALYS98
ASER99
ATHR171
AARG380
BGLU33
BMET84

site_idSWS_FT_FI2
Number of Residues6
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
BASN37
BASP79
BGLN119

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P15108
ChainResidueDetails
ASER657
BSER657

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PDB entries from 2024-07-24

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