Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1SX3

GroEL14-(ATPgammaS)14

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006457	biological_process	protein folding
A	0009314	biological_process	response to radiation
A	0009408	biological_process	response to heat
A	0016020	cellular_component	membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0019068	biological_process	virion assembly
A	0042026	biological_process	protein refolding
A	0042802	molecular_function	identical protein binding
A	0051082	molecular_function	unfolded protein binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
A	1990220	cellular_component	GroEL-GroES complex
B	0000287	molecular_function	magnesium ion binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006457	biological_process	protein folding
B	0009314	biological_process	response to radiation
B	0009408	biological_process	response to heat
B	0016020	cellular_component	membrane
B	0016887	molecular_function	ATP hydrolysis activity
B	0019068	biological_process	virion assembly
B	0042026	biological_process	protein refolding
B	0042802	molecular_function	identical protein binding
B	0051082	molecular_function	unfolded protein binding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
B	1990220	cellular_component	GroEL-GroES complex
C	0000287	molecular_function	magnesium ion binding
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006457	biological_process	protein folding
C	0009314	biological_process	response to radiation
C	0009408	biological_process	response to heat
C	0016020	cellular_component	membrane
C	0016887	molecular_function	ATP hydrolysis activity
C	0019068	biological_process	virion assembly
C	0042026	biological_process	protein refolding
C	0042802	molecular_function	identical protein binding
C	0051082	molecular_function	unfolded protein binding
C	0140662	molecular_function	ATP-dependent protein folding chaperone
C	1990220	cellular_component	GroEL-GroES complex
D	0000287	molecular_function	magnesium ion binding
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006457	biological_process	protein folding
D	0009314	biological_process	response to radiation
D	0009408	biological_process	response to heat
D	0016020	cellular_component	membrane
D	0016887	molecular_function	ATP hydrolysis activity
D	0019068	biological_process	virion assembly
D	0042026	biological_process	protein refolding
D	0042802	molecular_function	identical protein binding
D	0051082	molecular_function	unfolded protein binding
D	0140662	molecular_function	ATP-dependent protein folding chaperone
D	1990220	cellular_component	GroEL-GroES complex
E	0000287	molecular_function	magnesium ion binding
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006457	biological_process	protein folding
E	0009314	biological_process	response to radiation
E	0009408	biological_process	response to heat
E	0016020	cellular_component	membrane
E	0016887	molecular_function	ATP hydrolysis activity
E	0019068	biological_process	virion assembly
E	0042026	biological_process	protein refolding
E	0042802	molecular_function	identical protein binding
E	0051082	molecular_function	unfolded protein binding
E	0140662	molecular_function	ATP-dependent protein folding chaperone
E	1990220	cellular_component	GroEL-GroES complex
F	0000287	molecular_function	magnesium ion binding
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006457	biological_process	protein folding
F	0009314	biological_process	response to radiation
F	0009408	biological_process	response to heat
F	0016020	cellular_component	membrane
F	0016887	molecular_function	ATP hydrolysis activity
F	0019068	biological_process	virion assembly
F	0042026	biological_process	protein refolding
F	0042802	molecular_function	identical protein binding
F	0051082	molecular_function	unfolded protein binding
F	0140662	molecular_function	ATP-dependent protein folding chaperone
F	1990220	cellular_component	GroEL-GroES complex
G	0000287	molecular_function	magnesium ion binding
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0006457	biological_process	protein folding
G	0009314	biological_process	response to radiation
G	0009408	biological_process	response to heat
G	0016020	cellular_component	membrane
G	0016887	molecular_function	ATP hydrolysis activity
G	0019068	biological_process	virion assembly
G	0042026	biological_process	protein refolding
G	0042802	molecular_function	identical protein binding
G	0051082	molecular_function	unfolded protein binding
G	0140662	molecular_function	ATP-dependent protein folding chaperone
G	1990220	cellular_component	GroEL-GroES complex
H	0000287	molecular_function	magnesium ion binding
H	0005515	molecular_function	protein binding
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0006457	biological_process	protein folding
H	0009314	biological_process	response to radiation
H	0009408	biological_process	response to heat
H	0016020	cellular_component	membrane
H	0016887	molecular_function	ATP hydrolysis activity
H	0019068	biological_process	virion assembly
H	0042026	biological_process	protein refolding
H	0042802	molecular_function	identical protein binding
H	0051082	molecular_function	unfolded protein binding
H	0140662	molecular_function	ATP-dependent protein folding chaperone
H	1990220	cellular_component	GroEL-GroES complex
I	0000287	molecular_function	magnesium ion binding
I	0005515	molecular_function	protein binding
I	0005524	molecular_function	ATP binding
I	0005737	cellular_component	cytoplasm
I	0005829	cellular_component	cytosol
I	0006457	biological_process	protein folding
I	0009314	biological_process	response to radiation
I	0009408	biological_process	response to heat
I	0016020	cellular_component	membrane
I	0016887	molecular_function	ATP hydrolysis activity
I	0019068	biological_process	virion assembly
I	0042026	biological_process	protein refolding
I	0042802	molecular_function	identical protein binding
I	0051082	molecular_function	unfolded protein binding
I	0140662	molecular_function	ATP-dependent protein folding chaperone
I	1990220	cellular_component	GroEL-GroES complex
J	0000287	molecular_function	magnesium ion binding
J	0005515	molecular_function	protein binding
J	0005524	molecular_function	ATP binding
J	0005737	cellular_component	cytoplasm
J	0005829	cellular_component	cytosol
J	0006457	biological_process	protein folding
J	0009314	biological_process	response to radiation
J	0009408	biological_process	response to heat
J	0016020	cellular_component	membrane
J	0016887	molecular_function	ATP hydrolysis activity
J	0019068	biological_process	virion assembly
J	0042026	biological_process	protein refolding
J	0042802	molecular_function	identical protein binding
J	0051082	molecular_function	unfolded protein binding
J	0140662	molecular_function	ATP-dependent protein folding chaperone
J	1990220	cellular_component	GroEL-GroES complex
K	0000287	molecular_function	magnesium ion binding
K	0005515	molecular_function	protein binding
K	0005524	molecular_function	ATP binding
K	0005737	cellular_component	cytoplasm
K	0005829	cellular_component	cytosol
K	0006457	biological_process	protein folding
K	0009314	biological_process	response to radiation
K	0009408	biological_process	response to heat
K	0016020	cellular_component	membrane
K	0016887	molecular_function	ATP hydrolysis activity
K	0019068	biological_process	virion assembly
K	0042026	biological_process	protein refolding
K	0042802	molecular_function	identical protein binding
K	0051082	molecular_function	unfolded protein binding
K	0140662	molecular_function	ATP-dependent protein folding chaperone
K	1990220	cellular_component	GroEL-GroES complex
L	0000287	molecular_function	magnesium ion binding
L	0005515	molecular_function	protein binding
L	0005524	molecular_function	ATP binding
L	0005737	cellular_component	cytoplasm
L	0005829	cellular_component	cytosol
L	0006457	biological_process	protein folding
L	0009314	biological_process	response to radiation
L	0009408	biological_process	response to heat
L	0016020	cellular_component	membrane
L	0016887	molecular_function	ATP hydrolysis activity
L	0019068	biological_process	virion assembly
L	0042026	biological_process	protein refolding
L	0042802	molecular_function	identical protein binding
L	0051082	molecular_function	unfolded protein binding
L	0140662	molecular_function	ATP-dependent protein folding chaperone
L	1990220	cellular_component	GroEL-GroES complex
M	0000287	molecular_function	magnesium ion binding
M	0005515	molecular_function	protein binding
M	0005524	molecular_function	ATP binding
M	0005737	cellular_component	cytoplasm
M	0005829	cellular_component	cytosol
M	0006457	biological_process	protein folding
M	0009314	biological_process	response to radiation
M	0009408	biological_process	response to heat
M	0016020	cellular_component	membrane
M	0016887	molecular_function	ATP hydrolysis activity
M	0019068	biological_process	virion assembly
M	0042026	biological_process	protein refolding
M	0042802	molecular_function	identical protein binding
M	0051082	molecular_function	unfolded protein binding
M	0140662	molecular_function	ATP-dependent protein folding chaperone
M	1990220	cellular_component	GroEL-GroES complex
N	0000287	molecular_function	magnesium ion binding
N	0005515	molecular_function	protein binding
N	0005524	molecular_function	ATP binding
N	0005737	cellular_component	cytoplasm
N	0005829	cellular_component	cytosol
N	0006457	biological_process	protein folding
N	0009314	biological_process	response to radiation
N	0009408	biological_process	response to heat
N	0016020	cellular_component	membrane
N	0016887	molecular_function	ATP hydrolysis activity
N	0019068	biological_process	virion assembly
N	0042026	biological_process	protein refolding
N	0042802	molecular_function	identical protein binding
N	0051082	molecular_function	unfolded protein binding
N	0140662	molecular_function	ATP-dependent protein folding chaperone
N	1990220	cellular_component	GroEL-GroES complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 550

Chain	Residue
A	AGS1
A	ASP87
A	HOH561
A	HOH562

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K A 560

Chain	Residue
A	HOH565
A	HOH566
A	AGS1
A	THR30
A	LYS51
A	HOH563
A	HOH564

site_id	AC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE AGS A 1

Chain	Residue
A	THR30
A	LEU31
A	GLY32
A	PRO33
A	GLY53
A	ASP87
A	GLY88
A	THR89
A	THR90
A	THR91
A	GLY414
A	GLY415
A	ASN479
A	ALA480
A	ALA481
A	ILE493
A	ASP495
A	MG550
A	K560
A	HOH561
A	HOH562
A	HOH563
A	HOH579
A	HOH580

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 550

Chain	Residue
B	AGS1
B	ASP87
B	HOH561
B	HOH562

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K B 560

Chain	Residue
B	AGS1
B	THR30
B	LYS51
B	HOH563
B	HOH564
B	HOH565
B	HOH566

site_id	AC6
Number of Residues	22
Details	BINDING SITE FOR RESIDUE AGS B 1

Chain	Residue
B	THR30
B	LEU31
B	GLY32
B	PRO33
B	GLY53
B	ASP87
B	GLY88
B	THR89
B	THR90
B	THR91
B	GLY414
B	GLY415
B	ASN479
B	ALA480
B	ILE493
B	ASP495
B	MG550
B	K560
B	HOH562
B	HOH565
B	HOH566
B	HOH589

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 550

Chain	Residue
C	AGS1
C	ASP87
C	HOH561
C	HOH562

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE K C 560

Chain	Residue
C	AGS1
C	THR30
C	LYS51
C	HOH563
C	HOH564
C	HOH565
C	HOH566
C	HOH567

site_id	AC9
Number of Residues	24
Details	BINDING SITE FOR RESIDUE AGS C 1

Chain	Residue
C	K560
C	HOH561
C	HOH562
C	HOH566
C	HOH567
C	THR30
C	LEU31
C	GLY32
C	PRO33
C	GLY53
C	ASP87
C	GLY88
C	THR89
C	THR90
C	THR91
C	GLY414
C	GLY415
C	TYR478
C	ASN479
C	ALA480
C	ALA481
C	ILE493
C	ASP495
C	MG550

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K D 1

Chain	Residue
D	LYS132
D	ALA133
D	SER135

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 550

Chain	Residue
D	ASP87
D	AGS561
D	HOH562
D	HOH563

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K D 560

Chain	Residue
D	THR30
D	LYS51
D	AGS561
D	HOH564
D	HOH565
D	HOH566
D	HOH567

site_id	BC4
Number of Residues	25
Details	BINDING SITE FOR RESIDUE AGS D 561

Chain	Residue
D	THR30
D	LEU31
D	GLY32
D	PRO33
D	GLY53
D	ASP87
D	GLY88
D	THR89
D	THR90
D	THR91
D	GLY414
D	GLY415
D	TYR478
D	ASN479
D	ALA480
D	ALA481
D	ILE493
D	ASP495
D	MG550
D	K560
D	HOH563
D	HOH564
D	HOH567
D	HOH576
D	HOH579

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K E 527

Chain	Residue
B	ALA133
E	LYS132
E	ALA133
E	SER135

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 550

Chain	Residue
E	AGS1
E	ASP87
E	HOH561
E	HOH562

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K E 560

Chain	Residue
E	AGS1
E	THR30
E	LYS51
E	HOH563
E	HOH564
E	HOH565
E	HOH566

site_id	BC8
Number of Residues	26
Details	BINDING SITE FOR RESIDUE AGS E 1

Chain	Residue
E	THR30
E	LEU31
E	GLY32
E	PRO33
E	GLY53
E	ASP87
E	GLY88
E	THR89
E	THR90
E	THR91
E	GLY414
E	GLY415
E	TYR478
E	ASN479
E	ALA480
E	ALA481
E	ILE493
E	ASP495
E	MG550
E	K560
E	HOH561
E	HOH562
E	HOH563
E	HOH566
E	HOH568
E	HOH574

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG F 550

Chain	Residue
F	AGS1
F	ASP87
F	HOH561
F	HOH562

site_id	CC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K F 560

Chain	Residue
F	AGS1
F	THR30
F	LYS51
F	HOH563
F	HOH564
F	HOH565
F	HOH566

site_id	CC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE AGS F 1

Chain	Residue
F	THR30
F	LEU31
F	GLY32
F	PRO33
F	GLY53
F	ASP87
F	GLY88
F	THR89
F	THR90
F	THR91
F	GLY414
F	GLY415
F	TYR478
F	ASN479
F	ALA480
F	ALA481
F	ILE493
F	ASP495
F	MG550
F	K560
F	HOH562
F	HOH563
F	HOH566
F	HOH574
F	HOH581

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG G 550

Chain	Residue
G	AGS1
G	ASP87
G	HOH561
G	HOH562

site_id	CC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K G 560

Chain	Residue
G	AGS1
G	THR30
G	LYS51
G	HOH563
G	HOH564
G	HOH565
G	HOH566

site_id	CC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE AGS G 1

Chain	Residue
G	THR30
G	LEU31
G	GLY32
G	PRO33
G	GLY53
G	ASP87
G	GLY88
G	THR89
G	THR90
G	THR91
G	GLY414
G	GLY415
G	TYR478
G	ASN479
G	ALA480
G	ALA481
G	ILE493
G	ASP495
G	MG550
G	K560
G	HOH561
G	HOH562
G	HOH566
G	HOH575
G	HOH584

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG H 550

Chain	Residue
H	AGS1
H	ASP87
H	HOH561
H	HOH562

site_id	CC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K H 560

Chain	Residue
H	AGS1
H	THR30
H	LYS51
H	HOH563
H	HOH564
H	HOH565
H	HOH566

site_id	CC8
Number of Residues	26
Details	BINDING SITE FOR RESIDUE AGS H 1

Chain	Residue
H	THR30
H	LEU31
H	GLY32
H	PRO33
H	GLY53
H	ASP87
H	GLY88
H	THR89
H	THR90
H	THR91
H	GLY414
H	GLY415
H	ASN479
H	ALA480
H	ALA481
H	ILE493
H	ASP495
H	MG550
H	K560
H	HOH561
H	HOH562
H	HOH563
H	HOH565
H	HOH566
H	HOH577
H	HOH590

site_id	CC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG I 550

Chain	Residue
I	AGS1
I	ASP87
I	HOH561
I	HOH562

site_id	DC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K I 560

Chain	Residue
I	AGS1
I	THR30
I	LYS51
I	HOH563
I	HOH564
I	HOH565
I	HOH566

site_id	DC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE AGS I 1

Chain	Residue
I	THR30
I	LEU31
I	GLY32
I	PRO33
I	GLY53
I	ASP87
I	GLY88
I	THR89
I	THR90
I	THR91
I	GLY414
I	GLY415
I	ASN479
I	ALA480
I	ILE493
I	ASP495
I	MG550
I	K560
I	HOH561
I	HOH562
I	HOH563
I	HOH566
I	HOH575

site_id	DC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG J 550

Chain	Residue
J	AGS1
J	ASP87
J	HOH561
J	HOH562

site_id	DC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K J 560

Chain	Residue
J	AGS1
J	THR30
J	LYS51
J	HOH563
J	HOH564
J	HOH565
J	HOH566

site_id	DC5
Number of Residues	23
Details	BINDING SITE FOR RESIDUE AGS J 1

Chain	Residue
J	THR30
J	LEU31
J	GLY32
J	PRO33
J	GLY53
J	ASP87
J	GLY88
J	THR89
J	THR90
J	THR91
J	GLY414
J	GLY415
J	TYR478
J	ASN479
J	ALA480
J	ALA481
J	ASP495
J	MG550
J	K560
J	HOH561
J	HOH562
J	HOH566
J	HOH578

site_id	DC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG K 550

Chain	Residue
K	AGS1
K	ASP87
K	HOH561
K	HOH562

site_id	DC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K K 560

Chain	Residue
K	AGS1
K	THR30
K	LYS51
K	HOH563
K	HOH564
K	HOH565
K	HOH566

site_id	DC8
Number of Residues	23
Details	BINDING SITE FOR RESIDUE AGS K 1

Chain	Residue
K	THR30
K	LEU31
K	GLY32
K	PRO33
K	GLY53
K	ASP87
K	GLY88
K	THR89
K	THR90
K	THR91
K	GLY414
K	GLY415
K	TYR478
K	ASN479
K	ALA480
K	ALA481
K	ILE493
K	ASP495
K	MG550
K	K560
K	HOH561
K	HOH562
K	HOH582

site_id	DC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG L 550

Chain	Residue
L	AGS1
L	ASP87
L	HOH561
L	HOH562

site_id	EC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K L 560

Chain	Residue
L	AGS1
L	THR30
L	LYS51
L	HOH563
L	HOH564
L	HOH565
L	HOH566

site_id	EC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE AGS L 1

Chain	Residue
L	THR30
L	LEU31
L	GLY32
L	PRO33
L	GLY53
L	ASP87
L	GLY88
L	THR89
L	THR90
L	THR91
L	GLY414
L	GLY415
L	ASN479
L	ALA480
L	ALA481
L	ILE493
L	ASP495
L	MG550
L	K560
L	HOH562
L	HOH575
L	HOH584

site_id	EC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG M 550

Chain	Residue
M	AGS1
M	ASP87
M	HOH561
M	HOH562

site_id	EC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K M 560

Chain	Residue
M	AGS1
M	THR30
M	LYS51
M	HOH563
M	HOH564
M	HOH565
M	HOH566

site_id	EC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE AGS M 1

Chain	Residue
M	THR30
M	LEU31
M	GLY32
M	PRO33
M	ASP52
M	GLY53
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	MG550
M	K560
M	HOH561
M	HOH562
M	HOH566
M	HOH575

site_id	EC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG N 550

Chain	Residue
N	AGS1
N	ASP87
N	HOH561
N	HOH562

site_id	EC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K N 560

Chain	Residue
N	AGS1
N	THR30
N	LYS51
N	HOH563
N	HOH564
N	HOH565
N	HOH566

site_id	EC8
Number of Residues	22
Details	BINDING SITE FOR RESIDUE AGS N 1

Chain	Residue
N	THR30
N	GLY32
N	PRO33
N	GLY53
N	ASP87
N	GLY88
N	THR89
N	THR90
N	THR91
N	GLY414
N	GLY415
N	TYR478
N	ASN479
N	ALA480
N	ALA481
N	ILE493
N	ASP495
N	MG550
N	K560
N	HOH561
N	HOH562
N	HOH566

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ALA405-GLY416

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	154
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00600","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25174333","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14517228","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9285585","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1AON","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PCQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PF9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WVL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00600","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25174333","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14517228","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9285585","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1AON","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PF9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WVL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	70
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	14
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
A	THR90
A	ASP52
A	ASP398
A	THR89

site_id	CSA10
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
J	THR90
J	ASP52
J	ASP398
J	THR89

site_id	CSA11
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
K	THR90
K	ASP52
K	ASP398
K	THR89

site_id	CSA12
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
L	THR90
L	ASP52
L	ASP398
L	THR89

site_id	CSA13
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
M	THR90
M	ASP52
M	ASP398
M	THR89

site_id	CSA14
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
N	THR90
N	ASP52
N	ASP398
N	THR89

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
B	THR90
B	ASP52
B	ASP398
B	THR89

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
C	THR90
C	ASP52
C	ASP398
C	THR89

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
D	THR90
D	ASP52
D	ASP398
D	THR89

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
E	THR90
E	ASP52
E	ASP398
E	THR89

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
F	THR90
F	ASP52
F	ASP398
F	THR89

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
G	THR90
G	ASP52
G	ASP398
G	THR89

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
H	THR90
H	ASP52
H	ASP398
H	THR89

site_id	CSA9
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
I	THR90
I	ASP52
I	ASP398
I	THR89

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