Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3SN9

Fic protein from NEISSERIA MENINGITIDIS mutant S182A/E186A in complex with AMPPNP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0016779	molecular_function	nucleotidyltransferase activity
A	0018117	biological_process	protein adenylylation
A	0042803	molecular_function	protein homodimerization activity
A	0051302	biological_process	regulation of cell division
A	0070733	molecular_function	AMPylase activity
B	0005524	molecular_function	ATP binding
B	0016779	molecular_function	nucleotidyltransferase activity
B	0018117	biological_process	protein adenylylation
B	0042803	molecular_function	protein homodimerization activity
B	0051302	biological_process	regulation of cell division
B	0070733	molecular_function	AMPylase activity
C	0005524	molecular_function	ATP binding
C	0016779	molecular_function	nucleotidyltransferase activity
C	0018117	biological_process	protein adenylylation
C	0042803	molecular_function	protein homodimerization activity
C	0051302	biological_process	regulation of cell division
C	0070733	molecular_function	AMPylase activity
D	0005524	molecular_function	ATP binding
D	0016779	molecular_function	nucleotidyltransferase activity
D	0018117	biological_process	protein adenylylation
D	0042803	molecular_function	protein homodimerization activity
D	0051302	biological_process	regulation of cell division
D	0070733	molecular_function	AMPylase activity
E	0005524	molecular_function	ATP binding
E	0016779	molecular_function	nucleotidyltransferase activity
E	0018117	biological_process	protein adenylylation
E	0042803	molecular_function	protein homodimerization activity
E	0051302	biological_process	regulation of cell division
E	0070733	molecular_function	AMPylase activity
F	0005524	molecular_function	ATP binding
F	0016779	molecular_function	nucleotidyltransferase activity
F	0018117	biological_process	protein adenylylation
F	0042803	molecular_function	protein homodimerization activity
F	0051302	biological_process	regulation of cell division
F	0070733	molecular_function	AMPylase activity
G	0005524	molecular_function	ATP binding
G	0016779	molecular_function	nucleotidyltransferase activity
G	0018117	biological_process	protein adenylylation
G	0042803	molecular_function	protein homodimerization activity
G	0051302	biological_process	regulation of cell division
G	0070733	molecular_function	AMPylase activity
H	0005524	molecular_function	ATP binding
H	0016779	molecular_function	nucleotidyltransferase activity
H	0018117	biological_process	protein adenylylation
H	0042803	molecular_function	protein homodimerization activity
H	0051302	biological_process	regulation of cell division
H	0070733	molecular_function	AMPylase activity
I	0005524	molecular_function	ATP binding
I	0016779	molecular_function	nucleotidyltransferase activity
I	0018117	biological_process	protein adenylylation
I	0042803	molecular_function	protein homodimerization activity
I	0051302	biological_process	regulation of cell division
I	0070733	molecular_function	AMPylase activity
J	0005524	molecular_function	ATP binding
J	0016779	molecular_function	nucleotidyltransferase activity
J	0018117	biological_process	protein adenylylation
J	0042803	molecular_function	protein homodimerization activity
J	0051302	biological_process	regulation of cell division
J	0070733	molecular_function	AMPylase activity
K	0005524	molecular_function	ATP binding
K	0016779	molecular_function	nucleotidyltransferase activity
K	0018117	biological_process	protein adenylylation
K	0042803	molecular_function	protein homodimerization activity
K	0051302	biological_process	regulation of cell division
K	0070733	molecular_function	AMPylase activity
L	0005524	molecular_function	ATP binding
L	0016779	molecular_function	nucleotidyltransferase activity
L	0018117	biological_process	protein adenylylation
L	0042803	molecular_function	protein homodimerization activity
L	0051302	biological_process	regulation of cell division
L	0070733	molecular_function	AMPylase activity
M	0005524	molecular_function	ATP binding
M	0016779	molecular_function	nucleotidyltransferase activity
M	0018117	biological_process	protein adenylylation
M	0042803	molecular_function	protein homodimerization activity
M	0051302	biological_process	regulation of cell division
M	0070733	molecular_function	AMPylase activity
N	0005524	molecular_function	ATP binding
N	0016779	molecular_function	nucleotidyltransferase activity
N	0018117	biological_process	protein adenylylation
N	0042803	molecular_function	protein homodimerization activity
N	0051302	biological_process	regulation of cell division
N	0070733	molecular_function	AMPylase activity
O	0005524	molecular_function	ATP binding
O	0016779	molecular_function	nucleotidyltransferase activity
O	0018117	biological_process	protein adenylylation
O	0042803	molecular_function	protein homodimerization activity
O	0051302	biological_process	regulation of cell division
O	0070733	molecular_function	AMPylase activity
P	0005524	molecular_function	ATP binding
P	0016779	molecular_function	nucleotidyltransferase activity
P	0018117	biological_process	protein adenylylation
P	0042803	molecular_function	protein homodimerization activity
P	0051302	biological_process	regulation of cell division
P	0070733	molecular_function	AMPylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ANP A 300

Chain	Residue
A	LYS67
A	LYS140
A	TYR143
A	MET147
A	GLU148
A	PHE70
A	ASN104
A	HIS107
A	GLY112
A	ASN113
A	GLY114
A	ARG115
A	ARG118

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ANP B 300

Chain	Residue
B	LYS67
B	ASN104
B	HIS107
B	GLY112
B	ASN113
B	GLY114
B	ARG115
B	ARG118
B	LYS140
B	TYR143
B	MET147
B	GLU148

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ANP C 300

Chain	Residue
C	LYS67
C	ASN104
C	HIS107
C	GLY112
C	ASN113
C	GLY114
C	ARG115
C	ARG118
C	LYS140
C	TYR143
C	MET147
C	GLU148

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ANP D 300

Chain	Residue
D	LYS67
D	ASN104
D	HIS107
D	GLY112
D	ASN113
D	GLY114
D	ARG115
D	ARG118
D	LYS140
D	TYR143
D	MET147
D	GLU148

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ANP E 300

Chain	Residue
E	LYS67
E	PHE70
E	ASN104
E	HIS107
E	GLY112
E	ASN113
E	GLY114
E	ARG115
E	ARG118
E	TYR143
E	LEU144
E	MET147
E	GLU148

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ANP F 300

Chain	Residue
F	LYS67
F	ASN104
F	HIS107
F	GLY112
F	ASN113
F	GLY114
F	ARG115
F	ARG118
F	LYS140
F	TYR143
F	MET147
F	GLU148

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ANP G 300

Chain	Residue
G	LYS67
G	ASN104
G	HIS107
G	GLY112
G	ASN113
G	GLY114
G	ARG115
G	ARG118
G	LYS140
G	TYR143
G	MET147
G	GLU148

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ANP H 300

Chain	Residue
H	LYS67
H	ASN104
H	HIS107
H	GLY112
H	ASN113
H	GLY114
H	ARG115
H	ARG118
H	LYS140
H	TYR143
H	MET147
H	GLU148

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ANP I 300

Chain	Residue
I	ASN104
I	HIS107
I	GLY112
I	ASN113
I	GLY114
I	ARG115
I	ARG118
I	LYS140
I	TYR143
I	MET147
I	GLU148
I	LYS67

site_id	BC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ANP J 300

Chain	Residue
J	LYS67
J	PHE70
J	ASN104
J	HIS107
J	GLY112
J	ASN113
J	GLY114
J	ARG115
J	ARG118
J	LYS140
J	TYR143
J	MET147
J	GLU148

site_id	BC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ANP K 300

Chain	Residue
K	LYS67
K	PHE70
K	ASN104
K	HIS107
K	GLY112
K	ASN113
K	GLY114
K	ARG115
K	ARG118
K	LYS140
K	TYR143
K	MET147
K	GLU148

site_id	BC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ANP L 300

Chain	Residue
L	LYS67
L	PHE70
L	ASN104
L	HIS107
L	GLY112
L	ASN113
L	GLY114
L	ARG115
L	ARG118
L	TYR143
L	MET147
L	GLU148

site_id	BC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ANP M 300

Chain	Residue
M	LYS67
M	PHE70
M	ASN104
M	HIS107
M	GLY112
M	ASN113
M	GLY114
M	ARG115
M	ARG118
M	LYS140
M	TYR143
M	MET147
M	GLU148

site_id	BC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ANP N 300

Chain	Residue
N	LYS67
N	ASN104
N	HIS107
N	GLY112
N	ASN113
N	GLY114
N	ARG115
N	ARG118
N	LYS140
N	TYR143
N	MET147
N	GLU148

site_id	BC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ANP O 300

Chain	Residue
O	LYS67
O	ASN104
O	HIS107
O	GLY112
O	ASN113
O	GLY114
O	ARG115
O	ARG118
O	LYS140
O	TYR143
O	MET147
O	GLU148

site_id	BC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ANP P 300

Chain	Residue
P	LYS67
P	PHE70
P	ASN104
P	HIS107
P	GLY112
P	ASN113
P	GLY114
P	ARG115
P	ARG118
P	LYS140
P	TYR143
P	MET147

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	80
Details	BINDING: BINDING => ECO:0000269\|PubMed:22266942

Chain	Residue	Details
A	LYS67
B	ALA186
C	LYS67
C	ASN104
C	GLY112
C	LYS140
C	ALA186
D	LYS67
D	ASN104
D	GLY112
D	LYS140
A	ASN104
D	ALA186
E	LYS67
E	ASN104
E	GLY112
E	LYS140
E	ALA186
F	LYS67
F	ASN104
F	GLY112
F	LYS140
A	GLY112
F	ALA186
G	LYS67
G	ASN104
G	GLY112
G	LYS140
G	ALA186
H	LYS67
H	ASN104
H	GLY112
H	LYS140
A	LYS140
H	ALA186
I	LYS67
I	ASN104
I	GLY112
I	LYS140
I	ALA186
J	LYS67
J	ASN104
J	GLY112
J	LYS140
A	ALA186
J	ALA186
K	LYS67
K	ASN104
K	GLY112
K	LYS140
K	ALA186
L	LYS67
L	ASN104
L	GLY112
L	LYS140
B	LYS67
L	ALA186
M	LYS67
M	ASN104
M	GLY112
M	LYS140
M	ALA186
N	LYS67
N	ASN104
N	GLY112
N	LYS140
B	ASN104
N	ALA186
O	LYS67
O	ASN104
O	GLY112
O	LYS140
O	ALA186
P	LYS67
P	ASN104
P	GLY112
P	LYS140
B	GLY112
P	ALA186
B	LYS140

site_id	SWS_FT_FI2
Number of Residues	16
Details	MOD_RES: O-AMP-tyrosine; in vitro => ECO:0000269\|PubMed:22266942

Chain	Residue	Details
A	TYR183
J	TYR183
K	TYR183
L	TYR183
M	TYR183
N	TYR183
O	TYR183
P	TYR183
B	TYR183
C	TYR183
D	TYR183
E	TYR183
F	TYR183
G	TYR183
H	TYR183
I	TYR183

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