Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2V5H

Controlling the storage of nitrogen as arginine: the complex of PII and acetylglutamate kinase from Synechococcus elongatus PCC 7942

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003991	molecular_function	acetylglutamate kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006526	biological_process	L-arginine biosynthetic process
A	0008652	biological_process	amino acid biosynthetic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0042450	biological_process	L-arginine biosynthetic process via ornithine
A	0042802	molecular_function	identical protein binding
B	0000166	molecular_function	nucleotide binding
B	0003991	molecular_function	acetylglutamate kinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006526	biological_process	L-arginine biosynthetic process
B	0008652	biological_process	amino acid biosynthetic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0042450	biological_process	L-arginine biosynthetic process via ornithine
B	0042802	molecular_function	identical protein binding
C	0000166	molecular_function	nucleotide binding
C	0003991	molecular_function	acetylglutamate kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006526	biological_process	L-arginine biosynthetic process
C	0008652	biological_process	amino acid biosynthetic process
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0042450	biological_process	L-arginine biosynthetic process via ornithine
C	0042802	molecular_function	identical protein binding
D	0000166	molecular_function	nucleotide binding
D	0003991	molecular_function	acetylglutamate kinase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006526	biological_process	L-arginine biosynthetic process
D	0008652	biological_process	amino acid biosynthetic process
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0042450	biological_process	L-arginine biosynthetic process via ornithine
D	0042802	molecular_function	identical protein binding
E	0000166	molecular_function	nucleotide binding
E	0003991	molecular_function	acetylglutamate kinase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0006526	biological_process	L-arginine biosynthetic process
E	0008652	biological_process	amino acid biosynthetic process
E	0016301	molecular_function	kinase activity
E	0016740	molecular_function	transferase activity
E	0042450	biological_process	L-arginine biosynthetic process via ornithine
E	0042802	molecular_function	identical protein binding
F	0000166	molecular_function	nucleotide binding
F	0003991	molecular_function	acetylglutamate kinase activity
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0006526	biological_process	L-arginine biosynthetic process
F	0008652	biological_process	amino acid biosynthetic process
F	0016301	molecular_function	kinase activity
F	0016740	molecular_function	transferase activity
F	0042450	biological_process	L-arginine biosynthetic process via ornithine
F	0042802	molecular_function	identical protein binding
G	0000166	molecular_function	nucleotide binding
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005829	cellular_component	cytosol
G	0006808	biological_process	regulation of nitrogen utilization
G	0030234	molecular_function	enzyme regulator activity
G	0042802	molecular_function	identical protein binding
H	0000166	molecular_function	nucleotide binding
H	0005515	molecular_function	protein binding
H	0005524	molecular_function	ATP binding
H	0005829	cellular_component	cytosol
H	0006808	biological_process	regulation of nitrogen utilization
H	0030234	molecular_function	enzyme regulator activity
H	0042802	molecular_function	identical protein binding
I	0000166	molecular_function	nucleotide binding
I	0005515	molecular_function	protein binding
I	0005524	molecular_function	ATP binding
I	0005829	cellular_component	cytosol
I	0006808	biological_process	regulation of nitrogen utilization
I	0030234	molecular_function	enzyme regulator activity
I	0042802	molecular_function	identical protein binding
J	0000166	molecular_function	nucleotide binding
J	0005515	molecular_function	protein binding
J	0005524	molecular_function	ATP binding
J	0005829	cellular_component	cytosol
J	0006808	biological_process	regulation of nitrogen utilization
J	0030234	molecular_function	enzyme regulator activity
J	0042802	molecular_function	identical protein binding
K	0000166	molecular_function	nucleotide binding
K	0005515	molecular_function	protein binding
K	0005524	molecular_function	ATP binding
K	0005829	cellular_component	cytosol
K	0006808	biological_process	regulation of nitrogen utilization
K	0030234	molecular_function	enzyme regulator activity
K	0042802	molecular_function	identical protein binding
L	0000166	molecular_function	nucleotide binding
L	0005515	molecular_function	protein binding
L	0005524	molecular_function	ATP binding
L	0005829	cellular_component	cytosol
L	0006808	biological_process	regulation of nitrogen utilization
L	0030234	molecular_function	enzyme regulator activity
L	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE NLG A 1292

Chain	Residue
A	GLY69
A	ALA188
A	GLY70
A	GLY71
A	ILE74
A	ARG92
A	SER174
A	ASN185
A	ILE186
A	ASN187

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA A 1293

Chain	Residue
A	GLU277
A	THR280
A	HOH2027
A	HOH2028

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE NLG B 1297

Chain	Residue
B	GLY69
B	GLY70
B	GLY71
B	ILE74
B	ARG92
B	SER174
B	ASN185
B	ILE186
B	ALA188

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA B 1298

Chain	Residue
B	GLU277
B	THR280
B	HOH2022

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE NLG C 1292

Chain	Residue
C	GLY69
C	GLY70
C	GLY71
C	ILE74
C	ARG92
C	SER174
C	ASN185
C	ALA188

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA C 1293

Chain	Residue
C	GLU277
C	THR280
C	HOH2014
C	HOH2015

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NLG D 1294

Chain	Residue
D	GLY69
D	GLY70
D	GLY71
D	ILE74
D	ARG92
D	ASN185
D	ALA188

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA D 1295

Chain	Residue
D	GLU277
D	THR280

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NLG E 1294

Chain	Residue
E	GLY69
E	GLY70
E	GLY71
E	ILE74
E	ARG92
E	ASN185
E	ALA188

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL E 1295

Chain	Residue
D	GLY181
E	LYS112
E	ASP113
E	ARG117

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA E 1296

Chain	Residue
E	GLU277
E	THR280

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NLG F 1293

Chain	Residue
F	GLY69
F	GLY70
F	GLY71
F	ARG92
F	VAL149
F	ASN185
F	ALA188

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA F 1294

Chain	Residue
F	GLU277
F	THR280
F	HOH2022
F	HOH2023

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL G 1112

Chain	Residue
G	GLN39
G	GLY87
G	ASP88
I	ARG103

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL H 1109

Chain	Residue
G	ARG103
H	ILE86
H	GLY87
H	HOH2011

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL H 1110

Chain	Residue
H	ARG101
H	ARG103
I	ILE86
I	GLY87
I	ASP88
I	HOH2008

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL J 1111

Chain	Residue
J	ARG103
K	ILE86
K	GLY87

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL J 1112

Chain	Residue
J	ILE86
J	GLY87
L	ARG103

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL K 1109

Chain	Residue
K	ARG101
K	ARG103
L	GLY87
L	ASP88
L	HOH2010

Functional Information from PROSITE/UniProt

site_id	PS00496
Number of Residues	6
Details	PII_GLNB_UMP P-II protein uridylation site. YRGSEY

Chain	Residue	Details
G	TYR46-TYR51

site_id	PS00638
Number of Residues	14
Details	PII_GLNB_CTER P-II protein C-terminal region signature. TgeiGDGKIFVspV

Chain	Residue	Details
G	THR83-VAL96

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00082","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00082","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"7592328","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Modified residue: {"description":"O-UMP-tyrosine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00675","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1oh9

Chain	Residue	Details
A	GLY38
A	LYS35
A	LYS248
A	GLY71

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1oh9

Chain	Residue	Details
B	GLY38
B	LYS35
B	LYS248
B	GLY71

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1oh9

Chain	Residue	Details
C	GLY38
C	LYS35
C	LYS248
C	GLY71

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1oh9

Chain	Residue	Details
D	GLY38
D	LYS35
D	LYS248
D	GLY71

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1oh9

Chain	Residue	Details
E	GLY38
E	LYS35
E	LYS248
E	GLY71

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1oh9

Chain	Residue	Details
F	GLY38
F	LYS35
F	LYS248
F	GLY71

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