Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5UYX

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003730	molecular_function	mRNA 3'-UTR binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005813	cellular_component	centrosome
A	0005829	cellular_component	cytosol
A	0005832	cellular_component	chaperonin-containing T-complex
A	0005874	cellular_component	microtubule
A	0006457	biological_process	protein folding
A	0009615	biological_process	response to virus
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0031681	molecular_function	G-protein beta-subunit binding
A	0032212	biological_process	positive regulation of telomere maintenance via telomerase
A	0044183	molecular_function	protein folding chaperone
A	0044297	cellular_component	cell body
A	0048027	molecular_function	mRNA 5'-UTR binding
A	0048487	molecular_function	beta-tubulin binding
A	0050821	biological_process	protein stabilization
A	0051082	molecular_function	unfolded protein binding
A	0070062	cellular_component	extracellular exosome
A	0140662	molecular_function	ATP-dependent protein folding chaperone
A	1904871	biological_process	positive regulation of protein localization to Cajal body
A	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
B	0000166	molecular_function	nucleotide binding
B	0003730	molecular_function	mRNA 3'-UTR binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005813	cellular_component	centrosome
B	0005829	cellular_component	cytosol
B	0005832	cellular_component	chaperonin-containing T-complex
B	0005874	cellular_component	microtubule
B	0006457	biological_process	protein folding
B	0009615	biological_process	response to virus
B	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0031681	molecular_function	G-protein beta-subunit binding
B	0032212	biological_process	positive regulation of telomere maintenance via telomerase
B	0044183	molecular_function	protein folding chaperone
B	0044297	cellular_component	cell body
B	0048027	molecular_function	mRNA 5'-UTR binding
B	0048487	molecular_function	beta-tubulin binding
B	0050821	biological_process	protein stabilization
B	0051082	molecular_function	unfolded protein binding
B	0070062	cellular_component	extracellular exosome
B	0140662	molecular_function	ATP-dependent protein folding chaperone
B	1904871	biological_process	positive regulation of protein localization to Cajal body
B	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
C	0000166	molecular_function	nucleotide binding
C	0003730	molecular_function	mRNA 3'-UTR binding
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005813	cellular_component	centrosome
C	0005829	cellular_component	cytosol
C	0005832	cellular_component	chaperonin-containing T-complex
C	0005874	cellular_component	microtubule
C	0006457	biological_process	protein folding
C	0009615	biological_process	response to virus
C	0016787	molecular_function	hydrolase activity
C	0016887	molecular_function	ATP hydrolysis activity
C	0031681	molecular_function	G-protein beta-subunit binding
C	0032212	biological_process	positive regulation of telomere maintenance via telomerase
C	0044183	molecular_function	protein folding chaperone
C	0044297	cellular_component	cell body
C	0048027	molecular_function	mRNA 5'-UTR binding
C	0048487	molecular_function	beta-tubulin binding
C	0050821	biological_process	protein stabilization
C	0051082	molecular_function	unfolded protein binding
C	0070062	cellular_component	extracellular exosome
C	0140662	molecular_function	ATP-dependent protein folding chaperone
C	1904871	biological_process	positive regulation of protein localization to Cajal body
C	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
D	0000166	molecular_function	nucleotide binding
D	0003730	molecular_function	mRNA 3'-UTR binding
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005813	cellular_component	centrosome
D	0005829	cellular_component	cytosol
D	0005832	cellular_component	chaperonin-containing T-complex
D	0005874	cellular_component	microtubule
D	0006457	biological_process	protein folding
D	0009615	biological_process	response to virus
D	0016787	molecular_function	hydrolase activity
D	0016887	molecular_function	ATP hydrolysis activity
D	0031681	molecular_function	G-protein beta-subunit binding
D	0032212	biological_process	positive regulation of telomere maintenance via telomerase
D	0044183	molecular_function	protein folding chaperone
D	0044297	cellular_component	cell body
D	0048027	molecular_function	mRNA 5'-UTR binding
D	0048487	molecular_function	beta-tubulin binding
D	0050821	biological_process	protein stabilization
D	0051082	molecular_function	unfolded protein binding
D	0070062	cellular_component	extracellular exosome
D	0140662	molecular_function	ATP-dependent protein folding chaperone
D	1904871	biological_process	positive regulation of protein localization to Cajal body
D	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue ADP A 601

Chain	Residue
A	LEU52
A	GLU508
A	LYS513
A	GLY53
A	ASP104
A	GLY105
A	THR106
A	THR107
A	GLY422
A	CYS493
A	VAL506

site_id	AC2
Number of Residues	14
Details	binding site for residue ADP B 601

Chain	Residue
B	SER51
B	LEU52
B	GLY53
B	ASP104
B	GLY105
B	THR106
B	THR107
B	GLY108
B	GLY422
B	LEU462
B	CYS493
B	LEU494
B	VAL506
B	GLU508

site_id	AC3
Number of Residues	10
Details	binding site for residue ADP C 601

Chain	Residue
C	SER51
C	LEU52
C	GLY53
C	GLY105
C	THR106
C	THR107
C	GLY108
C	GLY422
C	CYS493
C	GLU508

site_id	AC4
Number of Residues	13
Details	binding site for residue ADP D 601

Chain	Residue
D	SER51
D	LEU52
D	GLY53
D	ASP104
D	GLY105
D	THR106
D	THR107
D	GLY108
D	GLY422
D	CYS493
D	LEU494
D	VAL506
D	GLU508

Functional Information from PROSITE/UniProt

site_id	PS00750
Number of Residues	13
Details	TCP1_1 Chaperonins TCP-1 signature 1. RTsLGPnGldKMM

Chain	Residue	Details
A	ARG49-MET61

site_id	PS00751
Number of Residues	17
Details	TCP1_2 Chaperonins TCP-1 signature 2. VTNDGATILsmMdVdHQ

Chain	Residue	Details
A	VAL70-GLN86

site_id	PS00995
Number of Residues	9
Details	TCP1_3 Chaperonins TCP-1 signature 3. QDdeIGDGT

Chain	Residue	Details
A	GLN98-THR106

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7X3J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"37193829","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7X0S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X0V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"36493755","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TTN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	25
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)