Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5F2V

Crystal structure of the small alarmone synthethase 1 from Bacillus subtilis bound to AMPCPP

Replaces: 5DEE

Functional Information from GO Data

Chain	GOid	namespace	contents
O	0005524	molecular_function	ATP binding
O	0005525	molecular_function	GTP binding
O	0008728	molecular_function	GTP diphosphokinase activity
O	0015969	biological_process	guanosine tetraphosphate metabolic process
O	0015970	biological_process	guanosine tetraphosphate biosynthetic process
O	0016301	molecular_function	kinase activity
O	0046872	molecular_function	metal ion binding
P	0005524	molecular_function	ATP binding
P	0005525	molecular_function	GTP binding
P	0008728	molecular_function	GTP diphosphokinase activity
P	0015969	biological_process	guanosine tetraphosphate metabolic process
P	0015970	biological_process	guanosine tetraphosphate biosynthetic process
P	0016301	molecular_function	kinase activity
P	0046872	molecular_function	metal ion binding
Q	0005524	molecular_function	ATP binding
Q	0005525	molecular_function	GTP binding
Q	0008728	molecular_function	GTP diphosphokinase activity
Q	0015969	biological_process	guanosine tetraphosphate metabolic process
Q	0015970	biological_process	guanosine tetraphosphate biosynthetic process
Q	0016301	molecular_function	kinase activity
Q	0046872	molecular_function	metal ion binding
R	0005524	molecular_function	ATP binding
R	0005525	molecular_function	GTP binding
R	0008728	molecular_function	GTP diphosphokinase activity
R	0015969	biological_process	guanosine tetraphosphate metabolic process
R	0015970	biological_process	guanosine tetraphosphate biosynthetic process
R	0016301	molecular_function	kinase activity
R	0046872	molecular_function	metal ion binding
S	0005524	molecular_function	ATP binding
S	0005525	molecular_function	GTP binding
S	0008728	molecular_function	GTP diphosphokinase activity
S	0015969	biological_process	guanosine tetraphosphate metabolic process
S	0015970	biological_process	guanosine tetraphosphate biosynthetic process
S	0016301	molecular_function	kinase activity
S	0046872	molecular_function	metal ion binding
T	0005524	molecular_function	ATP binding
T	0005525	molecular_function	GTP binding
T	0008728	molecular_function	GTP diphosphokinase activity
T	0015969	biological_process	guanosine tetraphosphate metabolic process
T	0015970	biological_process	guanosine tetraphosphate biosynthetic process
T	0016301	molecular_function	kinase activity
T	0046872	molecular_function	metal ion binding
U	0005524	molecular_function	ATP binding
U	0005525	molecular_function	GTP binding
U	0008728	molecular_function	GTP diphosphokinase activity
U	0015969	biological_process	guanosine tetraphosphate metabolic process
U	0015970	biological_process	guanosine tetraphosphate biosynthetic process
U	0016301	molecular_function	kinase activity
U	0046872	molecular_function	metal ion binding
V	0005524	molecular_function	ATP binding
V	0005525	molecular_function	GTP binding
V	0008728	molecular_function	GTP diphosphokinase activity
V	0015969	biological_process	guanosine tetraphosphate metabolic process
V	0015970	biological_process	guanosine tetraphosphate biosynthetic process
V	0016301	molecular_function	kinase activity
V	0046872	molecular_function	metal ion binding
W	0005524	molecular_function	ATP binding
W	0005525	molecular_function	GTP binding
W	0008728	molecular_function	GTP diphosphokinase activity
W	0015969	biological_process	guanosine tetraphosphate metabolic process
W	0015970	biological_process	guanosine tetraphosphate biosynthetic process
W	0016301	molecular_function	kinase activity
W	0046872	molecular_function	metal ion binding
X	0005524	molecular_function	ATP binding
X	0005525	molecular_function	GTP binding
X	0008728	molecular_function	GTP diphosphokinase activity
X	0015969	biological_process	guanosine tetraphosphate metabolic process
X	0015970	biological_process	guanosine tetraphosphate biosynthetic process
X	0016301	molecular_function	kinase activity
X	0046872	molecular_function	metal ion binding
Y	0005524	molecular_function	ATP binding
Y	0005525	molecular_function	GTP binding
Y	0008728	molecular_function	GTP diphosphokinase activity
Y	0015969	biological_process	guanosine tetraphosphate metabolic process
Y	0015970	biological_process	guanosine tetraphosphate biosynthetic process
Y	0016301	molecular_function	kinase activity
Y	0046872	molecular_function	metal ion binding
Z	0005524	molecular_function	ATP binding
Z	0005525	molecular_function	GTP binding
Z	0008728	molecular_function	GTP diphosphokinase activity
Z	0015969	biological_process	guanosine tetraphosphate metabolic process
Z	0015970	biological_process	guanosine tetraphosphate biosynthetic process
Z	0016301	molecular_function	kinase activity
Z	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue APC V 301

Chain	Residue
V	ARG46
V	GLU139
V	GLN141
V	HIS155
V	MG302
V	HOH403
V	HOH410
V	LYS48
V	SER52
V	LYS56
V	ARG59
V	ASP72
V	GLY75
V	LEU76
V	ARG77

site_id	AC2
Number of Residues	3
Details	binding site for residue MG V 302

Chain	Residue
V	ASP72
V	APC301
V	HOH410

site_id	AC3
Number of Residues	14
Details	binding site for residue APC X 301

Chain	Residue
X	ARG46
X	LYS48
X	SER52
X	LYS56
X	ARG59
X	ASP72
X	GLY75
X	LEU76
X	ARG77
X	GLU139
X	GLN141
X	HIS155
X	MG302
X	HOH408

site_id	AC4
Number of Residues	4
Details	binding site for residue MG X 302

Chain	Residue
X	ASP72
X	GLU139
X	APC301
X	HOH408

site_id	AC5
Number of Residues	18
Details	binding site for residue APC T 301

Chain	Residue
T	ARG46
T	LYS48
T	LYS56
T	ASP72
T	GLY75
T	LEU76
T	ARG77
T	TYR107
T	GLU139
T	GLN141
T	HIS155
T	MG302
T	HOH401
T	HOH402
T	HOH405
T	HOH406
T	HOH413
T	HOH416

site_id	AC6
Number of Residues	5
Details	binding site for residue MG T 302

Chain	Residue
T	ASP72
T	GLU139
T	APC301
T	HOH406
T	HOH413

site_id	AC7
Number of Residues	3
Details	binding site for residue MG S 301

Chain	Residue
S	ASP72
S	GLU139
S	APC302

site_id	AC8
Number of Residues	12
Details	binding site for residue APC S 302

Chain	Residue
S	ARG46
S	LYS48
S	SER52
S	LYS56
S	ASP72
S	GLY75
S	LEU76
S	ARG77
S	GLU139
S	GLN141
S	HIS155
S	MG301

site_id	AC9
Number of Residues	13
Details	binding site for residue APC Y 301

Chain	Residue
Y	ARG46
Y	LYS48
Y	SER52
Y	LYS56
Y	ARG59
Y	ASP72
Y	GLY75
Y	LEU76
Y	ARG77
Y	GLN141
Y	MG302
Y	HOH402
Y	HOH404

site_id	AD1
Number of Residues	6
Details	binding site for residue MG Y 302

Chain	Residue
Y	LYS56
Y	ASP72
Y	GLU139
Y	APC301
Y	HOH402
Y	HOH404

site_id	AD2
Number of Residues	13
Details	binding site for residue APC O 301

Chain	Residue
O	GLY75
O	LEU76
O	ARG77
O	GLU139
O	GLN141
O	HIS155
O	MG302
O	THR44
O	ARG46
O	LYS48
O	SER52
O	LYS56
O	ASP72

site_id	AD3
Number of Residues	3
Details	binding site for residue MG O 302

Chain	Residue
O	ASP72
O	GLU139
O	APC301

site_id	AD4
Number of Residues	13
Details	binding site for residue APC Z 301

Chain	Residue
Z	ARG43
Z	LYS45
Z	SER49
Z	LYS53
Z	ASP69
Z	GLY72
Z	LEU73
Z	ARG74
Z	GLU136
Z	GLN138
Z	HIS152
Z	MG302
Z	HOH401

site_id	AD5
Number of Residues	4
Details	binding site for residue MG Z 302

Chain	Residue
Z	LYS53
Z	ASP69
Z	GLU136
Z	APC301

site_id	AD6
Number of Residues	16
Details	binding site for residue APC W 301

Chain	Residue
W	ARG46
W	LYS48
W	SER52
W	LYS56
W	ARG59
W	ASP72
W	GLY75
W	LEU76
W	ARG77
W	GLU139
W	GLN141
W	MG302
W	HOH402
W	HOH405
W	HOH407
W	HOH412

site_id	AD7
Number of Residues	4
Details	binding site for residue MG W 302

Chain	Residue
W	LYS56
W	ASP72
W	APC301
W	HOH405

site_id	AD8
Number of Residues	15
Details	binding site for residue APC U 301

Chain	Residue
U	ARG46
U	LYS48
U	PRO49
U	SER52
U	LYS56
U	ARG59
U	ASP72
U	GLY75
U	LEU76
U	ARG77
U	GLU139
U	GLN141
U	HIS155
U	MG302
U	HOH401

site_id	AD9
Number of Residues	5
Details	binding site for residue MG U 302

Chain	Residue
U	ASP72
U	GLU139
U	GLN141
U	APC301
U	HOH401

site_id	AE1
Number of Residues	13
Details	binding site for residue APC P 301

Chain	Residue
P	ARG46
P	LYS48
P	SER52
P	LYS56
P	ARG59
P	ASP72
P	GLY75
P	LEU76
P	ARG77
P	GLU139
P	GLN141
P	HIS155
P	MG302

site_id	AE2
Number of Residues	4
Details	binding site for residue MG P 302

Chain	Residue
P	ASP72
P	GLU139
P	APC301
P	HOH404

site_id	AE3
Number of Residues	16
Details	binding site for residue APC R 301

Chain	Residue
R	ARG46
R	LYS48
R	SER52
R	LYS56
R	ARG59
R	ASP72
R	GLY75
R	LEU76
R	ARG77
R	GLU139
R	GLN141
R	HIS155
R	MG302
R	HOH402
R	HOH405
R	HOH409

site_id	AE4
Number of Residues	4
Details	binding site for residue MG R 302

Chain	Residue
R	ASP72
R	APC301
R	HOH402
R	HOH409

site_id	AE5
Number of Residues	12
Details	binding site for residue APC Q 301

Chain	Residue
Q	ARG46
Q	LYS48
Q	SER52
Q	LYS56
Q	ASP72
Q	GLY75
Q	LEU76
Q	ARG77
Q	GLU139
Q	GLN141
Q	HIS155
Q	MG302

site_id	AE6
Number of Residues	3
Details	binding site for residue MG Q 302

Chain	Residue
Q	ASP72
Q	GLU139
Q	APC301

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: Proton acceptor => ECO:0000305\|PubMed:26460002

Chain	Residue	Details
V	GLU139
P	GLU139
R	GLU139
Q	GLU139
X	GLU139
T	GLU139
S	GLU139
Y	GLU139
O	GLU139
Z	GLU136
W	GLU139
U	GLU139

site_id	SWS_FT_FI2
Number of Residues	108
Details	BINDING: BINDING => ECO:0000269\|PubMed:26460002, ECO:0007744\|PDB:5DED

Chain	Residue	Details
V	LYS21
X	LYS21
Q	LYS21
Q	GLU41
Q	ARG46
Q	ARG59
Q	ARG105
Q	LYS112
Q	HIS120
Q	ASN148
Q	ALA151
X	GLU41
X	ARG46
X	ARG59
X	ARG105
X	LYS112
X	HIS120
X	ASN148
X	ALA151
T	LYS21
V	GLU41
T	GLU41
T	ARG46
T	ARG59
T	ARG105
T	LYS112
T	HIS120
T	ASN148
T	ALA151
S	LYS21
S	GLU41
V	ARG46
S	ARG46
S	ARG59
S	ARG105
S	LYS112
S	HIS120
S	ASN148
S	ALA151
Y	LYS21
Y	GLU41
Y	ARG46
V	ARG59
Y	ARG59
Y	ARG105
Y	LYS112
Y	HIS120
Y	ASN148
Y	ALA151
O	LYS21
O	GLU41
O	ARG46
O	ARG59
V	ARG105
O	ARG105
O	LYS112
O	HIS120
O	ASN148
O	ALA151
Z	LYS18
Z	GLU38
Z	ARG43
Z	ARG56
Z	ARG102
V	LYS112
Z	LYS109
Z	HIS117
Z	ASN145
Z	ALA148
W	LYS21
W	GLU41
W	ARG46
W	ARG59
W	ARG105
W	LYS112
V	HIS120
W	HIS120
W	ASN148
W	ALA151
U	LYS21
U	GLU41
U	ARG46
U	ARG59
U	ARG105
U	LYS112
U	HIS120
V	ASN148
U	ASN148
U	ALA151
P	LYS21
P	GLU41
P	ARG46
P	ARG59
P	ARG105
P	LYS112
P	HIS120
P	ASN148
V	ALA151
P	ALA151
R	LYS21
R	GLU41
R	ARG46
R	ARG59
R	ARG105
R	LYS112
R	HIS120
R	ASN148
R	ALA151

site_id	SWS_FT_FI3
Number of Residues	36
Details	BINDING: BINDING => ECO:0000305\|PubMed:26460002, ECO:0007744\|PDB:5F2V

Chain	Residue	Details
V	SER52
S	SER52
S	LYS56
S	ARG77
Y	SER52
Y	LYS56
Y	ARG77
O	SER52
O	LYS56
O	ARG77
Z	SER49
V	LYS56
Z	LYS53
Z	ARG74
W	SER52
W	LYS56
W	ARG77
U	SER52
U	LYS56
U	ARG77
P	SER52
P	LYS56
V	ARG77
P	ARG77
R	SER52
R	LYS56
R	ARG77
Q	SER52
Q	LYS56
Q	ARG77
X	SER52
X	LYS56
X	ARG77
T	SER52
T	LYS56
T	ARG77

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:26460002

Chain	Residue	Details
V	ASP72
P	ASP72
R	ASP72
Q	ASP72
X	ASP72
T	ASP72
S	ASP72
Y	ASP72
O	ASP72
Z	ASP69
W	ASP72
U	ASP72

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