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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5UYX

Structure of Human T-complex protein 1 subunit epsilon (CCT5)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003730molecular_functionmRNA 3'-UTR binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0005832cellular_componentchaperonin-containing T-complex
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0006457biological_processprotein folding
A0007339biological_processbinding of sperm to zona pellucida
A0009615biological_processresponse to virus
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0031681molecular_functionG-protein beta-subunit binding
A0032212biological_processpositive regulation of telomere maintenance via telomerase
A0044183molecular_functionprotein folding chaperone
A0044297cellular_componentcell body
A0048027molecular_functionmRNA 5'-UTR binding
A0048487molecular_functionbeta-tubulin binding
A0050821biological_processprotein stabilization
A0051082molecular_functionunfolded protein binding
A0070062cellular_componentextracellular exosome
A0140662molecular_functionATP-dependent protein folding chaperone
A1904871biological_processpositive regulation of protein localization to Cajal body
A1904874biological_processpositive regulation of telomerase RNA localization to Cajal body
B0000166molecular_functionnucleotide binding
B0003730molecular_functionmRNA 3'-UTR binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005829cellular_componentcytosol
B0005832cellular_componentchaperonin-containing T-complex
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0006457biological_processprotein folding
B0007339biological_processbinding of sperm to zona pellucida
B0009615biological_processresponse to virus
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0031681molecular_functionG-protein beta-subunit binding
B0032212biological_processpositive regulation of telomere maintenance via telomerase
B0044183molecular_functionprotein folding chaperone
B0044297cellular_componentcell body
B0048027molecular_functionmRNA 5'-UTR binding
B0048487molecular_functionbeta-tubulin binding
B0050821biological_processprotein stabilization
B0051082molecular_functionunfolded protein binding
B0070062cellular_componentextracellular exosome
B0140662molecular_functionATP-dependent protein folding chaperone
B1904871biological_processpositive regulation of protein localization to Cajal body
B1904874biological_processpositive regulation of telomerase RNA localization to Cajal body
C0000166molecular_functionnucleotide binding
C0003730molecular_functionmRNA 3'-UTR binding
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005813cellular_componentcentrosome
C0005829cellular_componentcytosol
C0005832cellular_componentchaperonin-containing T-complex
C0005856cellular_componentcytoskeleton
C0005874cellular_componentmicrotubule
C0006457biological_processprotein folding
C0007339biological_processbinding of sperm to zona pellucida
C0009615biological_processresponse to virus
C0016787molecular_functionhydrolase activity
C0016887molecular_functionATP hydrolysis activity
C0031681molecular_functionG-protein beta-subunit binding
C0032212biological_processpositive regulation of telomere maintenance via telomerase
C0044183molecular_functionprotein folding chaperone
C0044297cellular_componentcell body
C0048027molecular_functionmRNA 5'-UTR binding
C0048487molecular_functionbeta-tubulin binding
C0050821biological_processprotein stabilization
C0051082molecular_functionunfolded protein binding
C0070062cellular_componentextracellular exosome
C0140662molecular_functionATP-dependent protein folding chaperone
C1904871biological_processpositive regulation of protein localization to Cajal body
C1904874biological_processpositive regulation of telomerase RNA localization to Cajal body
D0000166molecular_functionnucleotide binding
D0003730molecular_functionmRNA 3'-UTR binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005813cellular_componentcentrosome
D0005829cellular_componentcytosol
D0005832cellular_componentchaperonin-containing T-complex
D0005856cellular_componentcytoskeleton
D0005874cellular_componentmicrotubule
D0006457biological_processprotein folding
D0007339biological_processbinding of sperm to zona pellucida
D0009615biological_processresponse to virus
D0016787molecular_functionhydrolase activity
D0016887molecular_functionATP hydrolysis activity
D0031681molecular_functionG-protein beta-subunit binding
D0032212biological_processpositive regulation of telomere maintenance via telomerase
D0044183molecular_functionprotein folding chaperone
D0044297cellular_componentcell body
D0048027molecular_functionmRNA 5'-UTR binding
D0048487molecular_functionbeta-tubulin binding
D0050821biological_processprotein stabilization
D0051082molecular_functionunfolded protein binding
D0070062cellular_componentextracellular exosome
D0140662molecular_functionATP-dependent protein folding chaperone
D1904871biological_processpositive regulation of protein localization to Cajal body
D1904874biological_processpositive regulation of telomerase RNA localization to Cajal body
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue ADP A 601
ChainResidue
ALEU52
AGLU508
ALYS513
AGLY53
AASP104
AGLY105
ATHR106
ATHR107
AGLY422
ACYS493
AVAL506
site_idAC2
Number of Residues14
Detailsbinding site for residue ADP B 601
ChainResidue
BSER51
BLEU52
BGLY53
BASP104
BGLY105
BTHR106
BTHR107
BGLY108
BGLY422
BLEU462
BCYS493
BLEU494
BVAL506
BGLU508
site_idAC3
Number of Residues10
Detailsbinding site for residue ADP C 601
ChainResidue
CSER51
CLEU52
CGLY53
CGLY105
CTHR106
CTHR107
CGLY108
CGLY422
CCYS493
CGLU508
site_idAC4
Number of Residues13
Detailsbinding site for residue ADP D 601
ChainResidue
DSER51
DLEU52
DGLY53
DASP104
DGLY105
DTHR106
DTHR107
DGLY108
DGLY422
DCYS493
DLEU494
DVAL506
DGLU508
Functional Information from PROSITE/UniProt
site_idPS00750
Number of Residues13
DetailsTCP1_1 Chaperonins TCP-1 signature 1. RTsLGPnGldKMM
ChainResidueDetails
AARG49-MET61
site_idPS00751
Number of Residues17
DetailsTCP1_2 Chaperonins TCP-1 signature 2. VTNDGATILsmMdVdHQ
ChainResidueDetails
AVAL70-GLN86
site_idPS00995
Number of Residues9
DetailsTCP1_3 Chaperonins TCP-1 signature 3. QDdeIGDGT
ChainResidueDetails
AGLN98-THR106
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7X3J","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35449234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NVL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X3U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues25
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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