Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4B2T

The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning

Functional Information from GO Data

Chain	GOid	namespace	contents
a	0000166	molecular_function	nucleotide binding
a	0005524	molecular_function	ATP binding
a	0005813	cellular_component	centrosome
a	0005829	cellular_component	cytosol
a	0005832	cellular_component	chaperonin-containing T-complex
a	0006457	biological_process	protein folding
a	0016787	molecular_function	hydrolase activity
a	0016887	molecular_function	ATP hydrolysis activity
a	0046872	molecular_function	metal ion binding
a	0051082	molecular_function	unfolded protein binding
a	0140662	molecular_function	ATP-dependent protein folding chaperone
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0005813	cellular_component	centrosome
A	0005829	cellular_component	cytosol
A	0005832	cellular_component	chaperonin-containing T-complex
A	0006457	biological_process	protein folding
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0046872	molecular_function	metal ion binding
A	0051082	molecular_function	unfolded protein binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
b	0000166	molecular_function	nucleotide binding
b	0002199	cellular_component	zona pellucida receptor complex
b	0005515	molecular_function	protein binding
b	0005524	molecular_function	ATP binding
b	0005737	cellular_component	cytoplasm
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	0016787	molecular_function	hydrolase activity
b	0016887	molecular_function	ATP hydrolysis activity
b	0031625	molecular_function	ubiquitin protein ligase binding
b	0044183	molecular_function	protein folding chaperone
b	0044297	cellular_component	cell body
b	0046872	molecular_function	metal ion binding
b	0050821	biological_process	protein stabilization
b	0051082	molecular_function	unfolded protein binding
b	0140662	molecular_function	ATP-dependent protein folding chaperone
b	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
B	0000166	molecular_function	nucleotide binding
B	0002199	cellular_component	zona pellucida receptor complex
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
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	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0031625	molecular_function	ubiquitin protein ligase binding
B	0044183	molecular_function	protein folding chaperone
B	0044297	cellular_component	cell body
B	0046872	molecular_function	metal ion binding
B	0050821	biological_process	protein stabilization
B	0051082	molecular_function	unfolded protein binding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
B	1904874	biological_process	positive regulation of telomerase RNA localization to Cajal body
d	0000166	molecular_function	nucleotide binding
d	0005524	molecular_function	ATP binding
d	0005737	cellular_component	cytoplasm
d	0005813	cellular_component	centrosome
d	0005832	cellular_component	chaperonin-containing T-complex
d	0006457	biological_process	protein folding
d	0016787	molecular_function	hydrolase activity
d	0016887	molecular_function	ATP hydrolysis activity
d	0042470	cellular_component	melanosome
d	0046872	molecular_function	metal ion binding
d	0051082	molecular_function	unfolded protein binding
d	0140662	molecular_function	ATP-dependent protein folding chaperone
D	0000166	molecular_function	nucleotide binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005813	cellular_component	centrosome
D	0005832	cellular_component	chaperonin-containing T-complex
D	0006457	biological_process	protein folding
D	0016787	molecular_function	hydrolase activity
D	0016887	molecular_function	ATP hydrolysis activity
D	0042470	cellular_component	melanosome
D	0046872	molecular_function	metal ion binding
D	0051082	molecular_function	unfolded protein binding
D	0140662	molecular_function	ATP-dependent protein folding chaperone
e	0000166	molecular_function	nucleotide binding
e	0003730	molecular_function	mRNA 3'-UTR binding
e	0005515	molecular_function	protein binding
e	0005524	molecular_function	ATP binding
e	0005813	cellular_component	centrosome
e	0005832	cellular_component	chaperonin-containing T-complex
e	0005874	cellular_component	microtubule
e	0006457	biological_process	protein folding
e	0009615	biological_process	response to virus
e	0016787	molecular_function	hydrolase activity
e	0016887	molecular_function	ATP hydrolysis activity
e	0031681	molecular_function	G-protein beta-subunit binding
e	0044183	molecular_function	protein folding chaperone
e	0044297	cellular_component	cell body
e	0048027	molecular_function	mRNA 5'-UTR binding
e	0048487	molecular_function	beta-tubulin binding
e	0050821	biological_process	protein stabilization
e	0051082	molecular_function	unfolded protein binding
e	0140662	molecular_function	ATP-dependent protein folding chaperone
E	0000166	molecular_function	nucleotide binding
E	0003730	molecular_function	mRNA 3'-UTR binding
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005813	cellular_component	centrosome
E	0005832	cellular_component	chaperonin-containing T-complex
E	0005874	cellular_component	microtubule
E	0006457	biological_process	protein folding
E	0009615	biological_process	response to virus
E	0016787	molecular_function	hydrolase activity
E	0016887	molecular_function	ATP hydrolysis activity
E	0031681	molecular_function	G-protein beta-subunit binding
E	0044183	molecular_function	protein folding chaperone
E	0044297	cellular_component	cell body
E	0048027	molecular_function	mRNA 5'-UTR binding
E	0048487	molecular_function	beta-tubulin binding
E	0050821	biological_process	protein stabilization
E	0051082	molecular_function	unfolded protein binding
E	0140662	molecular_function	ATP-dependent protein folding chaperone
g	0000166	molecular_function	nucleotide binding
g	0002199	cellular_component	zona pellucida receptor complex
g	0005524	molecular_function	ATP binding
g	0005737	cellular_component	cytoplasm
g	0005832	cellular_component	chaperonin-containing T-complex
g	0005874	cellular_component	microtubule
g	0006457	biological_process	protein folding
g	0016787	molecular_function	hydrolase activity
g	0016887	molecular_function	ATP hydrolysis activity
g	0044183	molecular_function	protein folding chaperone
g	0044297	cellular_component	cell body
g	0046872	molecular_function	metal ion binding
g	0050821	biological_process	protein stabilization
g	0051082	molecular_function	unfolded protein binding
g	0140662	molecular_function	ATP-dependent protein folding chaperone
G	0000166	molecular_function	nucleotide binding
G	0002199	cellular_component	zona pellucida receptor complex
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0005832	cellular_component	chaperonin-containing T-complex
G	0005874	cellular_component	microtubule
G	0006457	biological_process	protein folding
G	0016787	molecular_function	hydrolase activity
G	0016887	molecular_function	ATP hydrolysis activity
G	0044183	molecular_function	protein folding chaperone
G	0044297	cellular_component	cell body
G	0046872	molecular_function	metal ion binding
G	0050821	biological_process	protein stabilization
G	0051082	molecular_function	unfolded protein binding
G	0140662	molecular_function	ATP-dependent protein folding chaperone
h	0000166	molecular_function	nucleotide binding
h	0005515	molecular_function	protein binding
h	0005524	molecular_function	ATP binding
h	0005737	cellular_component	cytoplasm
h	0005832	cellular_component	chaperonin-containing T-complex
h	0005874	cellular_component	microtubule
h	0006457	biological_process	protein folding
h	0016787	molecular_function	hydrolase activity
h	0016887	molecular_function	ATP hydrolysis activity
h	0042802	molecular_function	identical protein binding
h	0044183	molecular_function	protein folding chaperone
h	0044297	cellular_component	cell body
h	0046872	molecular_function	metal ion binding
h	0050821	biological_process	protein stabilization
h	0051082	molecular_function	unfolded protein binding
h	0140662	molecular_function	ATP-dependent protein folding chaperone
H	0000166	molecular_function	nucleotide binding
H	0005515	molecular_function	protein binding
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0005832	cellular_component	chaperonin-containing T-complex
H	0005874	cellular_component	microtubule
H	0006457	biological_process	protein folding
H	0016787	molecular_function	hydrolase activity
H	0016887	molecular_function	ATP hydrolysis activity
H	0042802	molecular_function	identical protein binding
H	0044183	molecular_function	protein folding chaperone
H	0044297	cellular_component	cell body
H	0046872	molecular_function	metal ion binding
H	0050821	biological_process	protein stabilization
H	0051082	molecular_function	unfolded protein binding
H	0140662	molecular_function	ATP-dependent protein folding chaperone
q	0000166	molecular_function	nucleotide binding
q	0005524	molecular_function	ATP binding
q	0005737	cellular_component	cytoplasm
q	0005813	cellular_component	centrosome
q	0005832	cellular_component	chaperonin-containing T-complex
q	0006457	biological_process	protein folding
q	0016787	molecular_function	hydrolase activity
q	0016887	molecular_function	ATP hydrolysis activity
q	0046872	molecular_function	metal ion binding
q	0051082	molecular_function	unfolded protein binding
q	0140662	molecular_function	ATP-dependent protein folding chaperone
Q	0000166	molecular_function	nucleotide binding
Q	0005524	molecular_function	ATP binding
Q	0005737	cellular_component	cytoplasm
Q	0005813	cellular_component	centrosome
Q	0005832	cellular_component	chaperonin-containing T-complex
Q	0006457	biological_process	protein folding
Q	0016787	molecular_function	hydrolase activity
Q	0016887	molecular_function	ATP hydrolysis activity
Q	0046872	molecular_function	metal ion binding
Q	0051082	molecular_function	unfolded protein binding
Q	0140662	molecular_function	ATP-dependent protein folding chaperone
z	0000166	molecular_function	nucleotide binding
z	0005524	molecular_function	ATP binding
z	0005737	cellular_component	cytoplasm
z	0005832	cellular_component	chaperonin-containing T-complex
z	0005874	cellular_component	microtubule
z	0006457	biological_process	protein folding
z	0016787	molecular_function	hydrolase activity
z	0016887	molecular_function	ATP hydrolysis activity
z	0044183	molecular_function	protein folding chaperone
z	0046872	molecular_function	metal ion binding
z	0050821	biological_process	protein stabilization
z	0051082	molecular_function	unfolded protein binding
z	0071987	molecular_function	WD40-repeat domain binding
z	0140662	molecular_function	ATP-dependent protein folding chaperone
Z	0000166	molecular_function	nucleotide binding
Z	0005524	molecular_function	ATP binding
Z	0005737	cellular_component	cytoplasm
Z	0005832	cellular_component	chaperonin-containing T-complex
Z	0005874	cellular_component	microtubule
Z	0006457	biological_process	protein folding
Z	0016787	molecular_function	hydrolase activity
Z	0016887	molecular_function	ATP hydrolysis activity
Z	0044183	molecular_function	protein folding chaperone
Z	0046872	molecular_function	metal ion binding
Z	0050821	biological_process	protein stabilization
Z	0051082	molecular_function	unfolded protein binding
Z	0071987	molecular_function	WD40-repeat domain binding
Z	0140662	molecular_function	ATP-dependent protein folding chaperone

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	26
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGDGTTSVTVlAaellreaesl........IAKK

Chain	Residue	Details
B	VAL95-LYS120

site_id	PS00141
Number of Residues	12
Details	ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. AIADTGANVVVT

Chain	Residue	Details
Q	ALA282-THR293

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

Chain	Residue	Details
E	LYS49-MET61
A	LYS33-LEU45
H	ARG37-ILE49
B	LYS40-LEU52
Q	ARG44-VAL56
D	ARG52-ILE64
G	ARG38-LEU50
Z	ARG35-LEU47

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

Chain	Residue	Details
E	VAL70-GLN86
A	ILE54-PRO70
H	ILE58-PRO74
B	VAL63-PRO79
Q	VAL65-PRO81
D	ILE73-PRO89
G	MET59-PRO75
Z	LEU56-PRO72

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

Chain	Residue	Details
E	GLN98-THR106
A	GLN82-THR90
H	GLN86-THR94
B	GLN91-THR99
Q	GLN93-THR101
D	GLN101-THR109
G	GLN87-THR95
Z	GLN84-THR92

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P17987","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P17987","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P17987","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P17987","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P11983","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P78371","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P78371","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P78371","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P50991","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P50991","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P80315","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P50991","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P50991","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	26
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P49368","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P49368","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P80318","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P49368","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P49368","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	6
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P49368","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q99832","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q99832","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"Q99832","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	26
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P50990","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	5
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P50990","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P50990","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	5
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P50990","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P50990","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"UniProtKB","id":"P50990","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P40227","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P80317","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P40227","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P40227","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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