Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4A13

model refined against symmetry-free cryo-EM map of TRiC-ADP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005832	cellular_component	chaperonin-containing T-complex
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
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005832	cellular_component	chaperonin-containing T-complex
C	0006457	biological_process	protein folding
C	0016887	molecular_function	ATP hydrolysis activity
C	0051082	molecular_function	unfolded protein binding
C	0140662	molecular_function	ATP-dependent protein folding chaperone
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005832	cellular_component	chaperonin-containing T-complex
D	0006457	biological_process	protein folding
D	0016887	molecular_function	ATP hydrolysis activity
D	0051082	molecular_function	unfolded protein binding
D	0140662	molecular_function	ATP-dependent protein folding chaperone
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0005832	cellular_component	chaperonin-containing T-complex
E	0006457	biological_process	protein folding
E	0016887	molecular_function	ATP hydrolysis activity
E	0051082	molecular_function	unfolded protein binding
E	0140662	molecular_function	ATP-dependent protein folding chaperone
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0005832	cellular_component	chaperonin-containing T-complex
F	0006457	biological_process	protein folding
F	0016887	molecular_function	ATP hydrolysis activity
F	0051082	molecular_function	unfolded protein binding
F	0140662	molecular_function	ATP-dependent protein folding chaperone
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
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	0005829	cellular_component	cytosol
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
I	0005515	molecular_function	protein binding
I	0005524	molecular_function	ATP binding
I	0005737	cellular_component	cytoplasm
I	0005829	cellular_component	cytosol
I	0005832	cellular_component	chaperonin-containing T-complex
I	0006457	biological_process	protein folding
I	0016887	molecular_function	ATP hydrolysis activity
I	0051082	molecular_function	unfolded protein binding
I	0140662	molecular_function	ATP-dependent protein folding chaperone
J	0005515	molecular_function	protein binding
J	0005524	molecular_function	ATP binding
J	0005737	cellular_component	cytoplasm
J	0005829	cellular_component	cytosol
J	0005832	cellular_component	chaperonin-containing T-complex
J	0006457	biological_process	protein folding
J	0016887	molecular_function	ATP hydrolysis activity
J	0051082	molecular_function	unfolded protein binding
J	0140662	molecular_function	ATP-dependent protein folding chaperone
K	0005515	molecular_function	protein binding
K	0005524	molecular_function	ATP binding
K	0005737	cellular_component	cytoplasm
K	0005829	cellular_component	cytosol
K	0005832	cellular_component	chaperonin-containing T-complex
K	0006457	biological_process	protein folding
K	0016887	molecular_function	ATP hydrolysis activity
K	0051082	molecular_function	unfolded protein binding
K	0140662	molecular_function	ATP-dependent protein folding chaperone
L	0005515	molecular_function	protein binding
L	0005524	molecular_function	ATP binding
L	0005737	cellular_component	cytoplasm
L	0005829	cellular_component	cytosol
L	0005832	cellular_component	chaperonin-containing T-complex
L	0006457	biological_process	protein folding
L	0016887	molecular_function	ATP hydrolysis activity
L	0051082	molecular_function	unfolded protein binding
L	0140662	molecular_function	ATP-dependent protein folding chaperone
M	0005515	molecular_function	protein binding
M	0005524	molecular_function	ATP binding
M	0005737	cellular_component	cytoplasm
M	0005829	cellular_component	cytosol
M	0005832	cellular_component	chaperonin-containing T-complex
M	0006457	biological_process	protein folding
M	0016887	molecular_function	ATP hydrolysis activity
M	0051082	molecular_function	unfolded protein binding
M	0140662	molecular_function	ATP-dependent protein folding chaperone
N	0005515	molecular_function	protein binding
N	0005524	molecular_function	ATP binding
N	0005737	cellular_component	cytoplasm
N	0005829	cellular_component	cytosol
N	0005832	cellular_component	chaperonin-containing T-complex
N	0006457	biological_process	protein folding
N	0016887	molecular_function	ATP hydrolysis activity
N	0051082	molecular_function	unfolded protein binding
N	0140662	molecular_function	ATP-dependent protein folding chaperone
O	0005515	molecular_function	protein binding
O	0005524	molecular_function	ATP binding
O	0005737	cellular_component	cytoplasm
O	0005829	cellular_component	cytosol
O	0005832	cellular_component	chaperonin-containing T-complex
O	0006457	biological_process	protein folding
O	0016887	molecular_function	ATP hydrolysis activity
O	0051082	molecular_function	unfolded protein binding
O	0140662	molecular_function	ATP-dependent protein folding chaperone
P	0005515	molecular_function	protein binding
P	0005524	molecular_function	ATP binding
P	0005737	cellular_component	cytoplasm
P	0005829	cellular_component	cytosol
P	0005832	cellular_component	chaperonin-containing T-complex
P	0006457	biological_process	protein folding
P	0016887	molecular_function	ATP hydrolysis activity
P	0051082	molecular_function	unfolded protein binding
P	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
A	VAL82-LYS107

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

Chain	Residue	Details
A	LYS27-LEU39

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

Chain	Residue	Details
A	VAL50-PRO66

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

Chain	Residue	Details
A	GLN78-THR86

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	32
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P78371

Chain	Residue	Details
A	SER47
E	SER247
F	SER47
F	SER247
G	SER47
G	SER247
H	SER47
H	SER247
I	SER47
I	SER247
J	SER47
A	SER247
J	SER247
K	SER47
K	SER247
L	SER47
L	SER247
M	SER47
M	SER247
N	SER47
N	SER247
O	SER47
B	SER47
O	SER247
P	SER47
P	SER247
B	SER247
C	SER47
C	SER247
D	SER47
D	SER247
E	SER47

site_id	SWS_FT_FI2
Number of Residues	32
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P78371

Chain	Residue	Details
A	LYS141
E	LYS168
F	LYS141
F	LYS168
G	LYS141
G	LYS168
H	LYS141
H	LYS168
I	LYS141
I	LYS168
J	LYS141
A	LYS168
J	LYS168
K	LYS141
K	LYS168
L	LYS141
L	LYS168
M	LYS141
M	LYS168
N	LYS141
N	LYS168
O	LYS141
B	LYS141
O	LYS168
P	LYS141
P	LYS168
B	LYS168
C	LYS141
C	LYS168
D	LYS141
D	LYS168
E	LYS141

site_id	SWS_FT_FI3
Number of Residues	16
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P78371

Chain	Residue	Details
A	THR248
J	THR248
K	THR248
L	THR248
M	THR248
N	THR248
O	THR248
P	THR248
B	THR248
C	THR248
D	THR248
E	THR248
F	THR248
G	THR248
H	THR248
I	THR248

site_id	SWS_FT_FI4
Number of Residues	32
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250\|UniProtKB:P78371

Chain	Residue	Details
A	LYS235
F	LYS235
G	LYS235
H	LYS235
I	LYS235
J	LYS235
K	LYS235
L	LYS235
M	LYS235
N	LYS235
O	LYS235
B	LYS235
P	LYS235
C	LYS235
D	LYS235
E	LYS235

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)