Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3J1F

Cryo-EM structure of 9-fold symmetric rATcpn-beta in ATP-binding state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0005832	cellular_component	chaperonin-containing T-complex
A	0006457	biological_process	protein folding
A	0016887	molecular_function	ATP hydrolysis activity
A	0042802	molecular_function	identical protein binding
A	0051082	molecular_function	unfolded protein binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
B	0005524	molecular_function	ATP binding
B	0005832	cellular_component	chaperonin-containing T-complex
B	0006457	biological_process	protein folding
B	0016887	molecular_function	ATP hydrolysis activity
B	0042802	molecular_function	identical protein binding
B	0051082	molecular_function	unfolded protein binding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
C	0005524	molecular_function	ATP binding
C	0005832	cellular_component	chaperonin-containing T-complex
C	0006457	biological_process	protein folding
C	0016887	molecular_function	ATP hydrolysis activity
C	0042802	molecular_function	identical protein binding
C	0051082	molecular_function	unfolded protein binding
C	0140662	molecular_function	ATP-dependent protein folding chaperone
D	0005524	molecular_function	ATP binding
D	0005832	cellular_component	chaperonin-containing T-complex
D	0006457	biological_process	protein folding
D	0016887	molecular_function	ATP hydrolysis activity
D	0042802	molecular_function	identical protein binding
D	0051082	molecular_function	unfolded protein binding
D	0140662	molecular_function	ATP-dependent protein folding chaperone
E	0005524	molecular_function	ATP binding
E	0005832	cellular_component	chaperonin-containing T-complex
E	0006457	biological_process	protein folding
E	0016887	molecular_function	ATP hydrolysis activity
E	0042802	molecular_function	identical protein binding
E	0051082	molecular_function	unfolded protein binding
E	0140662	molecular_function	ATP-dependent protein folding chaperone
F	0005524	molecular_function	ATP binding
F	0005832	cellular_component	chaperonin-containing T-complex
F	0006457	biological_process	protein folding
F	0016887	molecular_function	ATP hydrolysis activity
F	0042802	molecular_function	identical protein binding
F	0051082	molecular_function	unfolded protein binding
F	0140662	molecular_function	ATP-dependent protein folding chaperone
G	0005524	molecular_function	ATP binding
G	0005832	cellular_component	chaperonin-containing T-complex
G	0006457	biological_process	protein folding
G	0016887	molecular_function	ATP hydrolysis activity
G	0042802	molecular_function	identical protein binding
G	0051082	molecular_function	unfolded protein binding
G	0140662	molecular_function	ATP-dependent protein folding chaperone
H	0005524	molecular_function	ATP binding
H	0005832	cellular_component	chaperonin-containing T-complex
H	0006457	biological_process	protein folding
H	0016887	molecular_function	ATP hydrolysis activity
H	0042802	molecular_function	identical protein binding
H	0051082	molecular_function	unfolded protein binding
H	0140662	molecular_function	ATP-dependent protein folding chaperone
I	0005524	molecular_function	ATP binding
I	0005832	cellular_component	chaperonin-containing T-complex
I	0006457	biological_process	protein folding
I	0016887	molecular_function	ATP hydrolysis activity
I	0042802	molecular_function	identical protein binding
I	0051082	molecular_function	unfolded protein binding
I	0140662	molecular_function	ATP-dependent protein folding chaperone
K	0005524	molecular_function	ATP binding
K	0005832	cellular_component	chaperonin-containing T-complex
K	0006457	biological_process	protein folding
K	0016887	molecular_function	ATP hydrolysis activity
K	0042802	molecular_function	identical protein binding
K	0051082	molecular_function	unfolded protein binding
K	0140662	molecular_function	ATP-dependent protein folding chaperone
L	0005524	molecular_function	ATP binding
L	0005832	cellular_component	chaperonin-containing T-complex
L	0006457	biological_process	protein folding
L	0016887	molecular_function	ATP hydrolysis activity
L	0042802	molecular_function	identical protein binding
L	0051082	molecular_function	unfolded protein binding
L	0140662	molecular_function	ATP-dependent protein folding chaperone
M	0005524	molecular_function	ATP binding
M	0005832	cellular_component	chaperonin-containing T-complex
M	0006457	biological_process	protein folding
M	0016887	molecular_function	ATP hydrolysis activity
M	0042802	molecular_function	identical protein binding
M	0051082	molecular_function	unfolded protein binding
M	0140662	molecular_function	ATP-dependent protein folding chaperone
N	0005524	molecular_function	ATP binding
N	0005832	cellular_component	chaperonin-containing T-complex
N	0006457	biological_process	protein folding
N	0016887	molecular_function	ATP hydrolysis activity
N	0042802	molecular_function	identical protein binding
N	0051082	molecular_function	unfolded protein binding
N	0140662	molecular_function	ATP-dependent protein folding chaperone
O	0005524	molecular_function	ATP binding
O	0005832	cellular_component	chaperonin-containing T-complex
O	0006457	biological_process	protein folding
O	0016887	molecular_function	ATP hydrolysis activity
O	0042802	molecular_function	identical protein binding
O	0051082	molecular_function	unfolded protein binding
O	0140662	molecular_function	ATP-dependent protein folding chaperone
P	0005524	molecular_function	ATP binding
P	0005832	cellular_component	chaperonin-containing T-complex
P	0006457	biological_process	protein folding
P	0016887	molecular_function	ATP hydrolysis activity
P	0042802	molecular_function	identical protein binding
P	0051082	molecular_function	unfolded protein binding
P	0140662	molecular_function	ATP-dependent protein folding chaperone
Q	0005524	molecular_function	ATP binding
Q	0005832	cellular_component	chaperonin-containing T-complex
Q	0006457	biological_process	protein folding
Q	0016887	molecular_function	ATP hydrolysis activity
Q	0042802	molecular_function	identical protein binding
Q	0051082	molecular_function	unfolded protein binding
Q	0140662	molecular_function	ATP-dependent protein folding chaperone
R	0005524	molecular_function	ATP binding
R	0005832	cellular_component	chaperonin-containing T-complex
R	0006457	biological_process	protein folding
R	0016887	molecular_function	ATP hydrolysis activity
R	0042802	molecular_function	identical protein binding
R	0051082	molecular_function	unfolded protein binding
R	0140662	molecular_function	ATP-dependent protein folding chaperone
S	0005524	molecular_function	ATP binding
S	0005832	cellular_component	chaperonin-containing T-complex
S	0006457	biological_process	protein folding
S	0016887	molecular_function	ATP hydrolysis activity
S	0042802	molecular_function	identical protein binding
S	0051082	molecular_function	unfolded protein binding
S	0140662	molecular_function	ATP-dependent protein folding chaperone

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ATP A 800

Chain	Residue
A	TYR50
A	GLY418
A	LEU489
A	TYR490
A	GLU504
A	LYS509
A	MG801
A	PRO52
A	ALA101
A	ASP102
A	GLY103
A	THR104
A	LYS105
A	THR106
A	GLY417

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG A 801

Chain	Residue
A	ASP102
A	ATP800

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ATP B 800

Chain	Residue
B	TYR50
B	PRO52
B	ASP102
B	GLY103
B	THR104
B	LYS105
B	THR106
B	GLY418
B	ILE487
B	LEU489
B	MET497
B	GLU504
B	LYS509
B	MG801

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 801

Chain	Residue
B	ASP102
B	ATP800

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ATP C 800

Chain	Residue
C	TYR50
C	PRO52
C	ASP102
C	GLY103
C	THR104
C	LYS105
C	THR106
C	GLY417
C	GLY418
C	LEU489
C	VAL502
C	GLU504
C	LYS509
C	MG801

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 801

Chain	Residue
C	ASP102
C	GLY103
C	ATP800

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ATP D 800

Chain	Residue
D	TYR50
D	GLY51
D	ASP102
D	GLY103
D	THR104
D	LYS105
D	THR106
D	LYS172
D	GLY417
D	GLY418
D	ILE487
D	LEU489
D	MET497
D	GLU504
D	MG801

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG D 801

Chain	Residue
D	ASP102
D	ATP800

site_id	AC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ATP E 800

Chain	Residue
E	TYR50
E	ASP102
E	GLY103
E	THR104
E	LYS105
E	THR106
E	GLY417
E	GLY418
E	ILE487
E	LEU489
E	MET497
E	GLU504
E	LYS509
E	MG801

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG E 801

Chain	Residue
E	ASP102
E	ATP800

site_id	BC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ATP F 800

Chain	Residue
F	TYR50
F	GLY51
F	PRO52
F	ALA101
F	ASP102
F	GLY103
F	THR104
F	LYS105
F	THR106
F	GLY418
F	ILE487
F	LEU489
F	GLU504
F	LYS509
F	MG801

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG F 801

Chain	Residue
F	ATP800
F	ASP102

site_id	BC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ATP G 800

Chain	Residue
G	TYR50
G	GLY51
G	ASP102
G	GLY103
G	THR104
G	LYS105
G	THR106
G	GLY417
G	GLY418
G	ILE487
G	LEU489
G	VAL502
G	GLU504
G	LYS509
G	MG801

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG G 801

Chain	Residue
G	ASP102
G	ATP800

site_id	BC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ATP H 800

Chain	Residue
H	PRO52
H	ASP102
H	GLY103
H	THR104
H	LYS105
H	THR106
H	GLY418
H	LEU489
H	GLU504
H	LYS509
H	MG801

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG H 801

Chain	Residue
H	ASP102
H	ATP800

site_id	BC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ATP I 800

Chain	Residue
I	TYR50
I	GLY51
I	ASP102
I	GLY103
I	THR104
I	LYS105
I	THR106
I	SER171
I	GLY418
I	ILE487
I	LEU489
I	TYR490
I	GLU504
I	LYS509
I	MG801

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG I 801

Chain	Residue
I	ASP102
I	ATP800

site_id	CC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ATP K 800

Chain	Residue
K	TYR50
K	ASP102
K	GLY103
K	THR104
K	LYS105
K	THR106
K	GLY417
K	GLY418
K	ILE487
K	LEU489
K	GLU504
K	LYS509
K	MG801

site_id	CC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG K 801

Chain	Residue
K	ASP102
K	ATP800

site_id	CC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ATP L 800

Chain	Residue
L	TYR50
L	PRO52
L	ASP102
L	GLY103
L	THR104
L	LYS105
L	THR106
L	GLY417
L	GLY418
L	LEU458
L	ILE487
L	LEU489
L	GLU504
L	LYS509
L	MG801

site_id	CC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG L 801

Chain	Residue
L	ASP102
L	ATP800

site_id	CC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ATP M 800

Chain	Residue
M	TYR50
M	GLY51
M	PRO52
M	ASP102
M	GLY103
M	THR104
M	LYS105
M	THR106
M	GLY418
M	ILE487
M	LEU489
M	GLU504
M	LYS509
M	MG801

site_id	CC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG M 801

Chain	Residue
M	ASP102
M	ATP800

site_id	CC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ATP N 800

Chain	Residue
N	TYR50
N	GLY51
N	PRO52
N	ASP102
N	GLY103
N	THR104
N	LYS105
N	THR106
N	GLY417
N	GLY418
N	ILE487
N	LEU489
N	GLU504
N	MG801

site_id	CC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG N 801

Chain	Residue
N	ASP102
N	ATP800

site_id	CC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ATP O 800

Chain	Residue
O	TYR50
O	PRO52
O	ASP102
O	GLY103
O	THR104
O	LYS105
O	THR106
O	GLY418
O	ILE487
O	LEU489
O	GLU504
O	MG801

site_id	DC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG O 801

Chain	Residue
O	ASP102
O	ATP800

site_id	DC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ATP P 800

Chain	Residue
P	TYR50
P	GLY51
P	ASP102
P	GLY103
P	THR104
P	LYS105
P	THR106
P	GLY417
P	GLY418
P	ILE487
P	LEU489
P	MET497
P	GLU504
P	LYS509
P	MG801

site_id	DC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG P 801

Chain	Residue
P	ASP102
P	ATP800

site_id	DC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ATP Q 800

Chain	Residue
Q	TYR50
Q	PRO52
Q	ASP102
Q	GLY103
Q	THR104
Q	LYS105
Q	THR106
Q	GLY418
Q	ILE487
Q	TYR490
Q	MET497
Q	GLU504
Q	LYS509
Q	MG801

site_id	DC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG Q 801

Chain	Residue
Q	ASP102
Q	ATP800

site_id	DC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ATP R 800

Chain	Residue
R	TYR50
R	GLY51
R	PRO52
R	ASP102
R	GLY103
R	THR104
R	LYS105
R	THR106
R	GLY417
R	GLY418
R	ILE487
R	LEU489
R	MET497
R	GLU504
R	LYS509
R	MG801

site_id	DC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG R 801

Chain	Residue
R	ASP102
R	ATP800

site_id	DC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ATP S 800

Chain	Residue
S	TYR50
S	GLY51
S	ASP102
S	GLY103
S	THR104
S	LYS105
S	THR106
S	SER171
S	GLY418
S	VAL502
S	GLU504
S	LYS509
S	MG801

site_id	DC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG S 801

Chain	Residue
S	ASP102
S	ATP800

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LYS47-LEU59

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

Chain	Residue	Details
A	ILE68-PRO84

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

Chain	Residue	Details
A	GLN96-THR104

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