Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4PKN

Crystal structure of the football-shaped GroEL-GroES2-(ADPBeFx)14 complex containing substrate Rubisco

Functional Information from GO Data

Chain	GOid	namespace	contents
1	0005524	molecular_function	ATP binding
1	0005737	cellular_component	cytoplasm
1	0006457	biological_process	protein folding
1	0044183	molecular_function	protein folding chaperone
1	0046872	molecular_function	metal ion binding
1	0051082	molecular_function	unfolded protein binding
1	0051085	biological_process	chaperone cofactor-dependent protein refolding
1	0051087	molecular_function	protein-folding chaperone binding
2	0005524	molecular_function	ATP binding
2	0005737	cellular_component	cytoplasm
2	0006457	biological_process	protein folding
2	0044183	molecular_function	protein folding chaperone
2	0046872	molecular_function	metal ion binding
2	0051082	molecular_function	unfolded protein binding
2	0051085	biological_process	chaperone cofactor-dependent protein refolding
2	0051087	molecular_function	protein-folding chaperone binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006457	biological_process	protein folding
A	0009408	biological_process	response to heat
A	0016853	molecular_function	isomerase activity
A	0042026	biological_process	protein refolding
A	0046872	molecular_function	metal ion binding
A	0051082	molecular_function	unfolded protein binding
A	0051085	biological_process	chaperone cofactor-dependent protein refolding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
A	1990220	cellular_component	GroEL-GroES complex
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006457	biological_process	protein folding
B	0009408	biological_process	response to heat
B	0016853	molecular_function	isomerase activity
B	0042026	biological_process	protein refolding
B	0046872	molecular_function	metal ion binding
B	0051082	molecular_function	unfolded protein binding
B	0051085	biological_process	chaperone cofactor-dependent protein refolding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
B	1990220	cellular_component	GroEL-GroES complex
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006457	biological_process	protein folding
C	0009408	biological_process	response to heat
C	0016853	molecular_function	isomerase activity
C	0042026	biological_process	protein refolding
C	0046872	molecular_function	metal ion binding
C	0051082	molecular_function	unfolded protein binding
C	0051085	biological_process	chaperone cofactor-dependent protein refolding
C	0140662	molecular_function	ATP-dependent protein folding chaperone
C	1990220	cellular_component	GroEL-GroES complex
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006457	biological_process	protein folding
D	0009408	biological_process	response to heat
D	0016853	molecular_function	isomerase activity
D	0042026	biological_process	protein refolding
D	0046872	molecular_function	metal ion binding
D	0051082	molecular_function	unfolded protein binding
D	0051085	biological_process	chaperone cofactor-dependent protein refolding
D	0140662	molecular_function	ATP-dependent protein folding chaperone
D	1990220	cellular_component	GroEL-GroES complex
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0006457	biological_process	protein folding
E	0009408	biological_process	response to heat
E	0016853	molecular_function	isomerase activity
E	0042026	biological_process	protein refolding
E	0046872	molecular_function	metal ion binding
E	0051082	molecular_function	unfolded protein binding
E	0051085	biological_process	chaperone cofactor-dependent protein refolding
E	0140662	molecular_function	ATP-dependent protein folding chaperone
E	1990220	cellular_component	GroEL-GroES complex
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0006457	biological_process	protein folding
F	0009408	biological_process	response to heat
F	0016853	molecular_function	isomerase activity
F	0042026	biological_process	protein refolding
F	0046872	molecular_function	metal ion binding
F	0051082	molecular_function	unfolded protein binding
F	0051085	biological_process	chaperone cofactor-dependent protein refolding
F	0140662	molecular_function	ATP-dependent protein folding chaperone
F	1990220	cellular_component	GroEL-GroES complex
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0006457	biological_process	protein folding
G	0009408	biological_process	response to heat
G	0016853	molecular_function	isomerase activity
G	0042026	biological_process	protein refolding
G	0046872	molecular_function	metal ion binding
G	0051082	molecular_function	unfolded protein binding
G	0051085	biological_process	chaperone cofactor-dependent protein refolding
G	0140662	molecular_function	ATP-dependent protein folding chaperone
G	1990220	cellular_component	GroEL-GroES complex
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0006457	biological_process	protein folding
H	0009408	biological_process	response to heat
H	0016853	molecular_function	isomerase activity
H	0042026	biological_process	protein refolding
H	0046872	molecular_function	metal ion binding
H	0051082	molecular_function	unfolded protein binding
H	0051085	biological_process	chaperone cofactor-dependent protein refolding
H	0140662	molecular_function	ATP-dependent protein folding chaperone
H	1990220	cellular_component	GroEL-GroES complex
I	0005524	molecular_function	ATP binding
I	0005737	cellular_component	cytoplasm
I	0006457	biological_process	protein folding
I	0009408	biological_process	response to heat
I	0016853	molecular_function	isomerase activity
I	0042026	biological_process	protein refolding
I	0046872	molecular_function	metal ion binding
I	0051082	molecular_function	unfolded protein binding
I	0051085	biological_process	chaperone cofactor-dependent protein refolding
I	0140662	molecular_function	ATP-dependent protein folding chaperone
I	1990220	cellular_component	GroEL-GroES complex
J	0005524	molecular_function	ATP binding
J	0005737	cellular_component	cytoplasm
J	0006457	biological_process	protein folding
J	0009408	biological_process	response to heat
J	0016853	molecular_function	isomerase activity
J	0042026	biological_process	protein refolding
J	0046872	molecular_function	metal ion binding
J	0051082	molecular_function	unfolded protein binding
J	0051085	biological_process	chaperone cofactor-dependent protein refolding
J	0140662	molecular_function	ATP-dependent protein folding chaperone
J	1990220	cellular_component	GroEL-GroES complex
K	0005524	molecular_function	ATP binding
K	0005737	cellular_component	cytoplasm
K	0006457	biological_process	protein folding
K	0009408	biological_process	response to heat
K	0016853	molecular_function	isomerase activity
K	0042026	biological_process	protein refolding
K	0046872	molecular_function	metal ion binding
K	0051082	molecular_function	unfolded protein binding
K	0051085	biological_process	chaperone cofactor-dependent protein refolding
K	0140662	molecular_function	ATP-dependent protein folding chaperone
K	1990220	cellular_component	GroEL-GroES complex
L	0005524	molecular_function	ATP binding
L	0005737	cellular_component	cytoplasm
L	0006457	biological_process	protein folding
L	0009408	biological_process	response to heat
L	0016853	molecular_function	isomerase activity
L	0042026	biological_process	protein refolding
L	0046872	molecular_function	metal ion binding
L	0051082	molecular_function	unfolded protein binding
L	0051085	biological_process	chaperone cofactor-dependent protein refolding
L	0140662	molecular_function	ATP-dependent protein folding chaperone
L	1990220	cellular_component	GroEL-GroES complex
M	0005524	molecular_function	ATP binding
M	0005737	cellular_component	cytoplasm
M	0006457	biological_process	protein folding
M	0009408	biological_process	response to heat
M	0016853	molecular_function	isomerase activity
M	0042026	biological_process	protein refolding
M	0046872	molecular_function	metal ion binding
M	0051082	molecular_function	unfolded protein binding
M	0051085	biological_process	chaperone cofactor-dependent protein refolding
M	0140662	molecular_function	ATP-dependent protein folding chaperone
M	1990220	cellular_component	GroEL-GroES complex
N	0005524	molecular_function	ATP binding
N	0005737	cellular_component	cytoplasm
N	0006457	biological_process	protein folding
N	0009408	biological_process	response to heat
N	0016853	molecular_function	isomerase activity
N	0042026	biological_process	protein refolding
N	0046872	molecular_function	metal ion binding
N	0051082	molecular_function	unfolded protein binding
N	0051085	biological_process	chaperone cofactor-dependent protein refolding
N	0140662	molecular_function	ATP-dependent protein folding chaperone
N	1990220	cellular_component	GroEL-GroES complex
O	0005524	molecular_function	ATP binding
O	0005737	cellular_component	cytoplasm
O	0006457	biological_process	protein folding
O	0044183	molecular_function	protein folding chaperone
O	0046872	molecular_function	metal ion binding
O	0051082	molecular_function	unfolded protein binding
O	0051085	biological_process	chaperone cofactor-dependent protein refolding
O	0051087	molecular_function	protein-folding chaperone binding
P	0005524	molecular_function	ATP binding
P	0005737	cellular_component	cytoplasm
P	0006457	biological_process	protein folding
P	0044183	molecular_function	protein folding chaperone
P	0046872	molecular_function	metal ion binding
P	0051082	molecular_function	unfolded protein binding
P	0051085	biological_process	chaperone cofactor-dependent protein refolding
P	0051087	molecular_function	protein-folding chaperone binding
Q	0005524	molecular_function	ATP binding
Q	0005737	cellular_component	cytoplasm
Q	0006457	biological_process	protein folding
Q	0044183	molecular_function	protein folding chaperone
Q	0046872	molecular_function	metal ion binding
Q	0051082	molecular_function	unfolded protein binding
Q	0051085	biological_process	chaperone cofactor-dependent protein refolding
Q	0051087	molecular_function	protein-folding chaperone binding
R	0005524	molecular_function	ATP binding
R	0005737	cellular_component	cytoplasm
R	0006457	biological_process	protein folding
R	0044183	molecular_function	protein folding chaperone
R	0046872	molecular_function	metal ion binding
R	0051082	molecular_function	unfolded protein binding
R	0051085	biological_process	chaperone cofactor-dependent protein refolding
R	0051087	molecular_function	protein-folding chaperone binding
S	0005524	molecular_function	ATP binding
S	0005737	cellular_component	cytoplasm
S	0006457	biological_process	protein folding
S	0044183	molecular_function	protein folding chaperone
S	0046872	molecular_function	metal ion binding
S	0051082	molecular_function	unfolded protein binding
S	0051085	biological_process	chaperone cofactor-dependent protein refolding
S	0051087	molecular_function	protein-folding chaperone binding
T	0005524	molecular_function	ATP binding
T	0005737	cellular_component	cytoplasm
T	0006457	biological_process	protein folding
T	0044183	molecular_function	protein folding chaperone
T	0046872	molecular_function	metal ion binding
T	0051082	molecular_function	unfolded protein binding
T	0051085	biological_process	chaperone cofactor-dependent protein refolding
T	0051087	molecular_function	protein-folding chaperone binding
U	0005524	molecular_function	ATP binding
U	0005737	cellular_component	cytoplasm
U	0006457	biological_process	protein folding
U	0044183	molecular_function	protein folding chaperone
U	0046872	molecular_function	metal ion binding
U	0051082	molecular_function	unfolded protein binding
U	0051085	biological_process	chaperone cofactor-dependent protein refolding
U	0051087	molecular_function	protein-folding chaperone binding
V	0005524	molecular_function	ATP binding
V	0005737	cellular_component	cytoplasm
V	0006457	biological_process	protein folding
V	0044183	molecular_function	protein folding chaperone
V	0046872	molecular_function	metal ion binding
V	0051082	molecular_function	unfolded protein binding
V	0051085	biological_process	chaperone cofactor-dependent protein refolding
V	0051087	molecular_function	protein-folding chaperone binding
W	0005524	molecular_function	ATP binding
W	0005737	cellular_component	cytoplasm
W	0006457	biological_process	protein folding
W	0044183	molecular_function	protein folding chaperone
W	0046872	molecular_function	metal ion binding
W	0051082	molecular_function	unfolded protein binding
W	0051085	biological_process	chaperone cofactor-dependent protein refolding
W	0051087	molecular_function	protein-folding chaperone binding
X	0005524	molecular_function	ATP binding
X	0005737	cellular_component	cytoplasm
X	0006457	biological_process	protein folding
X	0044183	molecular_function	protein folding chaperone
X	0046872	molecular_function	metal ion binding
X	0051082	molecular_function	unfolded protein binding
X	0051085	biological_process	chaperone cofactor-dependent protein refolding
X	0051087	molecular_function	protein-folding chaperone binding
Y	0005524	molecular_function	ATP binding
Y	0005737	cellular_component	cytoplasm
Y	0006457	biological_process	protein folding
Y	0044183	molecular_function	protein folding chaperone
Y	0046872	molecular_function	metal ion binding
Y	0051082	molecular_function	unfolded protein binding
Y	0051085	biological_process	chaperone cofactor-dependent protein refolding
Y	0051087	molecular_function	protein-folding chaperone binding
Z	0005524	molecular_function	ATP binding
Z	0005737	cellular_component	cytoplasm
Z	0006457	biological_process	protein folding
Z	0044183	molecular_function	protein folding chaperone
Z	0046872	molecular_function	metal ion binding
Z	0051082	molecular_function	unfolded protein binding
Z	0051085	biological_process	chaperone cofactor-dependent protein refolding
Z	0051087	molecular_function	protein-folding chaperone binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	binding site for residue ADP G 601

Chain	Residue
G	THR30
G	THR91
G	GLY414
G	GLY415
G	ILE454
G	TYR478
G	ASN479
G	ALA480
G	ALA481
G	ILE493
G	ASP495
G	LEU31
G	BEF602
G	MG603
G	K604
G	GLY32
G	PRO33
G	LYS51
G	ASP87
G	GLY88
G	THR89
G	THR90

site_id	AC2
Number of Residues	10
Details	binding site for residue BEF G 602

Chain	Residue
G	ASP52
G	GLY53
G	GLY86
G	ASP87
G	THR89
G	THR90
G	ASP398
G	ADP601
G	MG603
G	K604

site_id	AC3
Number of Residues	3
Details	binding site for residue MG G 603

Chain	Residue
G	ASP87
G	ADP601
G	BEF602

site_id	AC4
Number of Residues	5
Details	binding site for residue K G 604

Chain	Residue
G	THR30
G	LYS51
G	THR90
G	ADP601
G	BEF602

site_id	AC5
Number of Residues	22
Details	binding site for residue ADP A 601

Chain	Residue
A	THR30
A	LEU31
A	GLY32
A	PRO33
A	LYS51
A	ASP87
A	GLY88
A	THR89
A	THR90
A	THR91
A	GLY414
A	GLY415
A	ILE454
A	TYR478
A	ASN479
A	ALA480
A	ALA481
A	ILE493
A	ASP495
A	BEF602
A	MG603
A	K604

site_id	AC6
Number of Residues	10
Details	binding site for residue BEF A 602

Chain	Residue
A	ASP52
A	GLY53
A	ASP87
A	GLY88
A	THR89
A	THR90
A	ASP398
A	ADP601
A	MG603
A	K604

site_id	AC7
Number of Residues	3
Details	binding site for residue MG A 603

Chain	Residue
A	ASP87
A	ADP601
A	BEF602

site_id	AC8
Number of Residues	5
Details	binding site for residue K A 604

Chain	Residue
A	THR30
A	LYS51
A	THR90
A	ADP601
A	BEF602

site_id	AC9
Number of Residues	20
Details	binding site for residue ADP B 601

Chain	Residue
B	K604
B	THR30
B	LEU31
B	GLY32
B	PRO33
B	LYS51
B	ASP87
B	GLY88
B	THR89
B	THR90
B	THR91
B	GLY414
B	GLY415
B	ILE454
B	ASN479
B	ALA480
B	ALA481
B	ASP495
B	BEF602
B	MG603

site_id	AD1
Number of Residues	11
Details	binding site for residue BEF B 602

Chain	Residue
B	THR30
B	LYS51
B	ASP52
B	GLY53
B	ASP87
B	THR89
B	THR90
B	ASP398
B	ADP601
B	MG603
B	K604

site_id	AD2
Number of Residues	4
Details	binding site for residue MG B 603

Chain	Residue
B	ASP87
B	SER151
B	ADP601
B	BEF602

site_id	AD3
Number of Residues	3
Details	binding site for residue K B 604

Chain	Residue
B	LYS51
B	ADP601
B	BEF602

site_id	AD4
Number of Residues	21
Details	binding site for residue ADP F 601

Chain	Residue
F	THR30
F	LEU31
F	GLY32
F	LYS51
F	ASP87
F	GLY88
F	THR89
F	THR90
F	THR91
F	GLY414
F	GLY415
F	ILE454
F	TYR478
F	ASN479
F	ALA480
F	ALA481
F	ILE493
F	ASP495
F	BEF602
F	MG603
F	K604

site_id	AD5
Number of Residues	11
Details	binding site for residue BEF F 602

Chain	Residue
F	ASP52
F	GLY53
F	GLY86
F	ASP87
F	GLY88
F	THR89
F	THR90
F	ASP398
F	ADP601
F	MG603
F	K604

site_id	AD6
Number of Residues	3
Details	binding site for residue MG F 603

Chain	Residue
F	ASP87
F	ADP601
F	BEF602

site_id	AD7
Number of Residues	5
Details	binding site for residue K F 604

Chain	Residue
F	THR30
F	LYS51
F	THR90
F	ADP601
F	BEF602

site_id	AD8
Number of Residues	19
Details	binding site for residue ADP E 601

Chain	Residue
E	THR30
E	LEU31
E	GLY32
E	LYS51
E	ASP87
E	GLY88
E	THR89
E	THR90
E	THR91
E	GLY414
E	GLY415
E	ILE454
E	TYR478
E	ASN479
E	ALA480
E	ASP495
E	BEF602
E	MG603
E	K604

site_id	AD9
Number of Residues	11
Details	binding site for residue BEF E 602

Chain	Residue
E	ASP52
E	GLY53
E	GLY86
E	ASP87
E	GLY88
E	THR89
E	THR90
E	ASP398
E	ADP601
E	MG603
E	K604

site_id	AE1
Number of Residues	3
Details	binding site for residue MG E 603

Chain	Residue
E	ASP87
E	ADP601
E	BEF602

site_id	AE2
Number of Residues	5
Details	binding site for residue K E 604

Chain	Residue
E	THR30
E	LYS51
E	THR90
E	ADP601
E	BEF602

site_id	AE3
Number of Residues	22
Details	binding site for residue ADP C 601

Chain	Residue
C	THR30
C	LEU31
C	GLY32
C	PRO33
C	LYS51
C	ASP87
C	GLY88
C	THR89
C	THR90
C	THR91
C	GLY414
C	GLY415
C	ILE454
C	TYR478
C	ASN479
C	ALA480
C	ALA481
C	ILE493
C	ASP495
C	BEF602
C	MG603
C	K604

site_id	AE4
Number of Residues	8
Details	binding site for residue BEF C 602

Chain	Residue
C	GLY53
C	ASP87
C	GLY88
C	THR89
C	THR90
C	ADP601
C	MG603
C	K604

site_id	AE5
Number of Residues	3
Details	binding site for residue MG C 603

Chain	Residue
C	ASP87
C	ADP601
C	BEF602

site_id	AE6
Number of Residues	5
Details	binding site for residue K C 604

Chain	Residue
C	THR30
C	LYS51
C	THR90
C	ADP601
C	BEF602

site_id	AE7
Number of Residues	22
Details	binding site for residue ADP D 601

Chain	Residue
D	THR30
D	LEU31
D	GLY32
D	PRO33
D	LYS51
D	ASP87
D	GLY88
D	THR89
D	THR90
D	THR91
D	GLY414
D	GLY415
D	ILE454
D	TYR478
D	ASN479
D	ALA480
D	ALA481
D	ILE493
D	ASP495
D	BEF602
D	MG603
D	K604

site_id	AE8
Number of Residues	9
Details	binding site for residue BEF D 602

Chain	Residue
D	ASP52
D	GLY53
D	ASP87
D	THR89
D	THR90
D	ASP398
D	ADP601
D	MG603
D	K604

site_id	AE9
Number of Residues	3
Details	binding site for residue MG D 603

Chain	Residue
D	ASP87
D	ADP601
D	BEF602

site_id	AF1
Number of Residues	5
Details	binding site for residue K D 604

Chain	Residue
D	THR30
D	LYS51
D	THR90
D	ADP601
D	BEF602

site_id	AF2
Number of Residues	21
Details	binding site for residue ADP K 601

Chain	Residue
K	THR30
K	LEU31
K	GLY32
K	LYS51
K	ASP87
K	GLY88
K	THR89
K	THR90
K	THR91
K	GLY414
K	GLY415
K	ILE454
K	TYR478
K	ASN479
K	ALA480
K	ALA481
K	ILE493
K	ASP495
K	BEF602
K	MG603
K	K604

site_id	AF3
Number of Residues	11
Details	binding site for residue BEF K 602

Chain	Residue
K	ASP52
K	GLY53
K	GLY86
K	ASP87
K	GLY88
K	THR89
K	THR90
K	ASP398
K	ADP601
K	MG603
K	K604

site_id	AF4
Number of Residues	3
Details	binding site for residue MG K 603

Chain	Residue
K	ASP87
K	ADP601
K	BEF602

site_id	AF5
Number of Residues	5
Details	binding site for residue K K 604

Chain	Residue
K	THR30
K	LYS51
K	THR90
K	ADP601
K	BEF602

site_id	AF6
Number of Residues	20
Details	binding site for residue ADP J 601

Chain	Residue
J	THR30
J	LEU31
J	GLY32
J	PRO33
J	LYS51
J	ASP87
J	GLY88
J	THR89
J	THR90
J	THR91
J	GLY415
J	ILE454
J	TYR478
J	ASN479
J	ALA480
J	ALA481
J	ASP495
J	BEF602
J	MG603
J	K604

site_id	AF7
Number of Residues	11
Details	binding site for residue BEF J 602

Chain	Residue
J	LYS51
J	ASP52
J	GLY53
J	ASP87
J	GLY88
J	THR89
J	THR90
J	ASP398
J	ADP601
J	MG603
J	K604

site_id	AF8
Number of Residues	3
Details	binding site for residue MG J 603

Chain	Residue
J	ASP87
J	ADP601
J	BEF602

site_id	AF9
Number of Residues	5
Details	binding site for residue K J 604

Chain	Residue
J	THR30
J	LYS51
J	THR90
J	ADP601
J	BEF602

site_id	AG1
Number of Residues	21
Details	binding site for residue ADP I 601

Chain	Residue
I	THR30
I	LEU31
I	GLY32
I	PRO33
I	LYS51
I	ASP87
I	GLY88
I	THR89
I	THR90
I	THR91
I	GLY414
I	GLY415
I	ILE454
I	TYR478
I	ASN479
I	ALA480
I	ALA481
I	ASP495
I	BEF602
I	MG603
I	K604

site_id	AG2
Number of Residues	9
Details	binding site for residue BEF I 602

Chain	Residue
I	ASP52
I	GLY86
I	ASP87
I	THR89
I	THR90
I	ASP398
I	ADP601
I	MG603
I	K604

site_id	AG3
Number of Residues	3
Details	binding site for residue MG I 603

Chain	Residue
I	ASP87
I	ADP601
I	BEF602

site_id	AG4
Number of Residues	5
Details	binding site for residue K I 604

Chain	Residue
I	THR30
I	LYS51
I	THR90
I	ADP601
I	BEF602

site_id	AG5
Number of Residues	19
Details	binding site for residue ADP L 601

Chain	Residue
L	THR30
L	LEU31
L	GLY32
L	LYS51
L	ASP87
L	GLY88
L	THR90
L	THR91
L	GLY415
L	ILE454
L	TYR478
L	ASN479
L	ALA480
L	ALA481
L	ILE493
L	ASP495
L	BEF602
L	MG603
L	K604

site_id	AG6
Number of Residues	10
Details	binding site for residue BEF L 602

Chain	Residue
L	LYS51
L	ASP52
L	GLY53
L	ASP87
L	GLY88
L	THR89
L	ASP398
L	ADP601
L	MG603
L	K604

site_id	AG7
Number of Residues	4
Details	binding site for residue MG L 603

Chain	Residue
L	ASP87
L	SER151
L	ADP601
L	BEF602

site_id	AG8
Number of Residues	5
Details	binding site for residue K L 604

Chain	Residue
L	THR30
L	LYS51
L	THR90
L	ADP601
L	BEF602

site_id	AG9
Number of Residues	21
Details	binding site for residue ADP M 601

Chain	Residue
M	THR30
M	LEU31
M	GLY32
M	PRO33
M	LYS51
M	ASP87
M	GLY88
M	THR89
M	THR90
M	THR91
M	GLY414
M	GLY415
M	TYR478
M	ASN479
M	ALA480
M	ALA481
M	ILE493
M	ASP495
M	BEF602
M	MG603
M	K604

site_id	AH1
Number of Residues	10
Details	binding site for residue BEF M 602

Chain	Residue
M	ASP52
M	GLY53
M	ASP87
M	GLY88
M	THR89
M	THR90
M	ASP398
M	ADP601
M	MG603
M	K604

site_id	AH2
Number of Residues	4
Details	binding site for residue MG M 603

Chain	Residue
M	ASP87
M	SER151
M	ADP601
M	BEF602

site_id	AH3
Number of Residues	5
Details	binding site for residue K M 604

Chain	Residue
M	THR30
M	LYS51
M	THR90
M	ADP601
M	BEF602

site_id	AH4
Number of Residues	22
Details	binding site for residue ADP H 601

Chain	Residue
H	THR30
H	LEU31
H	GLY32
H	PRO33
H	LYS51
H	ASP87
H	GLY88
H	THR89
H	THR90
H	THR91
H	GLY414
H	GLY415
H	ILE454
H	TYR478
H	ASN479
H	ALA480
H	ALA481
H	ILE493
H	ASP495
H	BEF602
H	MG603
H	K604

site_id	AH5
Number of Residues	10
Details	binding site for residue BEF H 602

Chain	Residue
H	THR30
H	LYS51
H	ASP52
H	GLY53
H	ASP87
H	THR89
H	THR90
H	ADP601
H	MG603
H	K604

site_id	AH6
Number of Residues	3
Details	binding site for residue MG H 603

Chain	Residue
H	ASP87
H	ADP601
H	BEF602

site_id	AH7
Number of Residues	4
Details	binding site for residue K H 604

Chain	Residue
H	THR30
H	LYS51
H	ADP601
H	BEF602

site_id	AH8
Number of Residues	21
Details	binding site for residue ADP N 601

Chain	Residue
N	THR30
N	LEU31
N	GLY32
N	PRO33
N	ASP87
N	GLY88
N	THR89
N	THR90
N	THR91
N	GLY414
N	GLY415
N	ILE454
N	TYR478
N	ASN479
N	ALA480
N	ALA481
N	ILE493
N	ASP495
N	BEF602
N	MG603
N	K604

site_id	AH9
Number of Residues	12
Details	binding site for residue BEF N 602

Chain	Residue
N	THR30
N	LYS51
N	ASP52
N	GLY53
N	ASP87
N	GLY88
N	THR89
N	THR90
N	ASP398
N	ADP601
N	MG603
N	K604

site_id	AI1
Number of Residues	3
Details	binding site for residue MG N 603

Chain	Residue
N	ASP87
N	ADP601
N	BEF602

site_id	AI2
Number of Residues	4
Details	binding site for residue K N 604

Chain	Residue
N	THR30
N	LYS51
N	ADP601
N	BEF602

Functional Information from PROSITE/UniProt

site_id	PS00296
Number of Residues	12
Details	CHAPERONINS_CPN60 Chaperonins cpn60 signature. AAVEEGVVaGGG

Chain	Residue	Details
G	ALA405-GLY416

site_id	PS00681
Number of Residues	25
Details	CHAPERONINS_CPN10 Chaperonins cpn10 signature. IrPLhDRVIVKrkevetksaGgIVL

Chain	Residue	Details
2	ILE3-LEU27

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