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	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	0005856	cellular_component	cytoskeleton
a	0006457	biological_process	protein folding
a	0016887	molecular_function	ATP hydrolysis activity
a	0051082	molecular_function	unfolded protein binding
a	0140662	molecular_function	ATP-dependent protein folding chaperone
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	0005856	cellular_component	cytoskeleton
A	0006457	biological_process	protein folding
A	0016887	molecular_function	ATP hydrolysis activity
A	0051082	molecular_function	unfolded protein binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
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	0006457	biological_process	protein folding
b	0016887	molecular_function	ATP hydrolysis activity
b	0051082	molecular_function	unfolded protein binding
b	0140662	molecular_function	ATP-dependent protein folding chaperone
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	0006457	biological_process	protein folding
B	0016887	molecular_function	ATP hydrolysis activity
B	0051082	molecular_function	unfolded protein binding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
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	0005856	cellular_component	cytoskeleton
d	0005929	cellular_component	cilium
d	0006457	biological_process	protein folding
d	0016887	molecular_function	ATP hydrolysis activity
d	0042470	cellular_component	melanosome
d	0051082	molecular_function	unfolded protein binding
d	0140662	molecular_function	ATP-dependent protein folding chaperone
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	0005856	cellular_component	cytoskeleton
D	0005929	cellular_component	cilium
D	0006457	biological_process	protein folding
D	0016887	molecular_function	ATP hydrolysis activity
D	0042470	cellular_component	melanosome
D	0051082	molecular_function	unfolded protein binding
D	0140662	molecular_function	ATP-dependent protein folding chaperone
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	0007339	biological_process	binding of sperm to zona pellucida
e	0009615	biological_process	response to virus
e	0016887	molecular_function	ATP hydrolysis activity
e	0031681	molecular_function	G-protein beta-subunit binding
e	0032212	biological_process	positive regulation of telomere maintenance via telomerase
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	0061077	biological_process	chaperone-mediated protein folding
e	0140662	molecular_function	ATP-dependent protein folding chaperone
e	1904851	biological_process	positive regulation of establishment of protein localization to telomere
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	0007339	biological_process	binding of sperm to zona pellucida
E	0009615	biological_process	response to virus
E	0016887	molecular_function	ATP hydrolysis activity
E	0031681	molecular_function	G-protein beta-subunit binding
E	0032212	biological_process	positive regulation of telomere maintenance via telomerase
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	0061077	biological_process	chaperone-mediated protein folding
E	0140662	molecular_function	ATP-dependent protein folding chaperone
E	1904851	biological_process	positive regulation of establishment of protein localization to telomere
g	0005524	molecular_function	ATP binding
g	0005737	cellular_component	cytoplasm
g	0005832	cellular_component	chaperonin-containing T-complex
g	0006457	biological_process	protein folding
g	0016887	molecular_function	ATP hydrolysis activity
g	0051082	molecular_function	unfolded protein binding
g	0140662	molecular_function	ATP-dependent protein folding chaperone
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0005832	cellular_component	chaperonin-containing T-complex
G	0006457	biological_process	protein folding
G	0016887	molecular_function	ATP hydrolysis activity
G	0051082	molecular_function	unfolded protein binding
G	0140662	molecular_function	ATP-dependent protein folding chaperone
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	0006457	biological_process	protein folding
h	0016887	molecular_function	ATP hydrolysis activity
h	0051082	molecular_function	unfolded protein binding
h	0140662	molecular_function	ATP-dependent protein folding chaperone
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	0006457	biological_process	protein folding
H	0016887	molecular_function	ATP hydrolysis activity
H	0051082	molecular_function	unfolded protein binding
H	0140662	molecular_function	ATP-dependent protein folding chaperone
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	0005856	cellular_component	cytoskeleton
q	0005929	cellular_component	cilium
q	0006457	biological_process	protein folding
q	0016887	molecular_function	ATP hydrolysis activity
q	0051082	molecular_function	unfolded protein binding
q	0140662	molecular_function	ATP-dependent protein folding chaperone
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	0005856	cellular_component	cytoskeleton
Q	0005929	cellular_component	cilium
Q	0006457	biological_process	protein folding
Q	0016887	molecular_function	ATP hydrolysis activity
Q	0051082	molecular_function	unfolded protein binding
Q	0140662	molecular_function	ATP-dependent protein folding chaperone
z	0005524	molecular_function	ATP binding
z	0005737	cellular_component	cytoplasm
z	0005832	cellular_component	chaperonin-containing T-complex
z	0006457	biological_process	protein folding
z	0016887	molecular_function	ATP hydrolysis activity
z	0051082	molecular_function	unfolded protein binding
z	0140662	molecular_function	ATP-dependent protein folding chaperone
Z	0005524	molecular_function	ATP binding
Z	0005737	cellular_component	cytoplasm
Z	0005832	cellular_component	chaperonin-containing T-complex
Z	0006457	biological_process	protein folding
Z	0016887	molecular_function	ATP hydrolysis activity
Z	0051082	molecular_function	unfolded protein 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. RTnLGPkGtmKML

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

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

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

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

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

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: N-acetylalanine => ECO:0000250\|UniProtKB:P40227

Chain	Residue	Details
Z	ALA2
z	ALA1002

site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P80317

Chain	Residue	Details
Z	LYS5
q	SER1537
Z	LYS287
z	LYS1005
z	LYS1287
Q	SER537
q	SER1023
q	SER1162
q	SER1269
q	SER1317

site_id	SWS_FT_FI3
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P40227

Chain	Residue	Details
Z	LYS199
Z	LYS365
Z	LYS377
Z	LYS388
z	LYS1199
z	LYS1365
z	LYS1377
z	LYS1388

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P40227

Chain	Residue	Details
Z	SER205
z	SER1205
Q	LYS466
q	LYS1318
q	LYS1400
q	LYS1466
d	LYS1322
d	LYS1329

site_id	SWS_FT_FI5
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250\|UniProtKB:P40227

Chain	Residue	Details
Z	LYS251
q	LYS1260
q	LYS1534
q	LYS1539
g	TYR1247
z	LYS1251
Q	LYS260
Q	LYS534
Q	LYS539
q	LYS1224
q	LYS1254

site_id	SWS_FT_FI6
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0000250\|UniProtKB:P50990

Chain	Residue	Details
Q	LYS459
q	LYS1459
g	THR1430
g	THR1459

site_id	SWS_FT_FI7
Number of Residues	10
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250\|UniProtKB:P49368

Chain	Residue	Details
G	LYS15
g	LYS1381
G	LYS248
G	LYS249
G	LYS381
g	LYS1015
g	LYS1248
g	LYS1249

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