Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3KO1

Cystal structure of thermosome from Acidianus tengchongensis strain S5

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
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	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	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	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	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	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	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	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	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

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ADP A 800

Chain	Residue
A	TYR50
A	LYS509
A	GLY51
A	GLY103
A	LYS105
A	THR106
A	SER171
A	GLY417
A	GLY418
A	GLU504

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ADP B 800

Chain	Residue
B	TYR50
B	GLY51
B	GLY103
B	LYS105
B	THR106
B	SER171
B	GLY417
B	GLY418
B	GLU504
B	LYS509

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ADP C 800

Chain	Residue
C	TYR50
C	GLY51
C	GLY103
C	LYS105
C	THR106
C	SER171
C	GLY417
C	GLY418
C	GLU504
C	LYS509

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ADP D 800

Chain	Residue
D	TYR50
D	GLY51
D	GLY103
D	LYS105
D	THR106
D	SER171
D	GLY417
D	GLY418
D	GLU504
D	LYS509

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ADP E 800

Chain	Residue
E	TYR50
E	GLY51
E	GLY103
E	LYS105
E	THR106
E	SER171
E	GLY417
E	GLY418
E	GLU504
E	LYS509

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ADP F 800

Chain	Residue
F	TYR50
F	GLY51
F	GLY103
F	LYS105
F	THR106
F	SER171
F	GLY417
F	GLY418
F	GLU504
F	LYS509

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ADP G 800

Chain	Residue
G	TYR50
G	GLY51
G	GLY103
G	LYS105
G	THR106
G	SER171
G	GLY417
G	GLY418
G	GLU504
G	LYS509

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ADP H 800

Chain	Residue
H	TYR50
H	GLY51
H	GLY103
H	LYS105
H	THR106
H	SER171
H	GLY417
H	GLY418
H	GLU504
H	LYS509

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ADP I 800

Chain	Residue
I	TYR50
I	GLY51
I	GLY103
I	LYS105
I	THR106
I	SER171
I	GLY417
I	GLY418
I	GLU504
I	LYS509

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)
		EDMap 2fo-fc (MTZ)