Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2XUL

Structure of PII from Synechococcus elongatus in complex with 2- oxoglutarate at high 2-OG concentrations

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005829	cellular_component	cytosol
A	0006351	biological_process	DNA-templated transcription
A	0006808	biological_process	regulation of nitrogen utilization
A	0030234	molecular_function	enzyme regulator activity
A	0042802	molecular_function	identical protein binding
B	0000166	molecular_function	nucleotide binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005829	cellular_component	cytosol
B	0006351	biological_process	DNA-templated transcription
B	0006808	biological_process	regulation of nitrogen utilization
B	0030234	molecular_function	enzyme regulator activity
B	0042802	molecular_function	identical protein binding
C	0000166	molecular_function	nucleotide binding
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005829	cellular_component	cytosol
C	0006351	biological_process	DNA-templated transcription
C	0006808	biological_process	regulation of nitrogen utilization
C	0030234	molecular_function	enzyme regulator activity
C	0042802	molecular_function	identical protein binding
D	0000166	molecular_function	nucleotide binding
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005829	cellular_component	cytosol
D	0006351	biological_process	DNA-templated transcription
D	0006808	biological_process	regulation of nitrogen utilization
D	0030234	molecular_function	enzyme regulator activity
D	0042802	molecular_function	identical protein binding
E	0000166	molecular_function	nucleotide binding
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005829	cellular_component	cytosol
E	0006351	biological_process	DNA-templated transcription
E	0006808	biological_process	regulation of nitrogen utilization
E	0030234	molecular_function	enzyme regulator activity
E	0042802	molecular_function	identical protein binding
F	0000166	molecular_function	nucleotide binding
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005829	cellular_component	cytosol
F	0006351	biological_process	DNA-templated transcription
F	0006808	biological_process	regulation of nitrogen utilization
F	0030234	molecular_function	enzyme regulator activity
F	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ATP A 200

Chain	Residue
A	ILE7
A	GLY89
A	LYS90
A	AKG201
A	MG202
A	HOH2039
A	HOH2040
B	MET28
B	THR29
B	GLU62
B	VAL64
A	GLY35
B	ARG101
B	ARG103
B	HOH2046
A	PHE36
A	GLY37
A	ARG38
A	GLN39
A	ILE86
A	GLY87
A	ASP88

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE AKG A 201

Chain	Residue
A	ARG9
A	PHE36
A	GLY37
A	ARG38
A	GLN39
A	LYS40
A	GLY41
A	LEU56
A	LYS58
A	ILE86
A	GLY87
A	ATP200
A	MG202
A	HOH2039

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 202

Chain	Residue
A	GLN39
A	ATP200
A	AKG201

site_id	AC4
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ATP B 200

Chain	Residue
B	ILE7
B	GLY35
B	PHE36
B	GLY37
B	ARG38
B	GLN39
B	ILE86
B	GLY87
B	ASP88
B	GLY89
B	LYS90
B	AKG201
B	MG202
B	HOH2049
C	GLY27
C	MET28
C	THR29
C	GLU62
C	ILE63
C	VAL64
C	ARG101
C	ARG103
C	HOH2013
C	HOH2014
C	HOH2031

site_id	AC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE AKG B 201

Chain	Residue
B	ARG9
B	PHE36
B	GLY37
B	ARG38
B	GLN39
B	LYS40
B	GLY41
B	GLN42
B	LEU56
B	LYS58
B	ILE86
B	GLY87
B	ATP200
B	MG202
B	HOH2049
B	HOH2050

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG B 202

Chain	Residue
B	GLN39
B	ATP200
B	AKG201

site_id	AC7
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ATP C 200

Chain	Residue
C	GLY89
C	LYS90
C	AKG201
C	MG202
C	HOH2038
C	HOH2039
C	HOH2040
A	GLY27
A	MET28
A	THR29
A	GLU62
A	VAL64
A	ARG101
A	ARG103
C	ILE7
C	GLY35
C	PHE36
C	GLY37
C	ARG38
C	GLN39
C	ILE86
C	GLY87
C	ASP88

site_id	AC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE AKG C 201

Chain	Residue
C	ARG9
C	PHE36
C	GLY37
C	ARG38
C	GLN39
C	LYS40
C	GLY41
C	LEU56
C	LYS58
C	ILE86
C	GLY87
C	ATP200
C	MG202
C	HOH2038
C	HOH2041

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 202

Chain	Residue
C	GLN39
C	GLY87
C	ATP200
C	AKG201

site_id	BC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ATP D 200

Chain	Residue
D	ILE7
D	GLY35
D	PHE36
D	GLY37
D	ARG38
D	GLN39
D	ILE86
D	GLY87
D	ASP88
D	GLY89
D	LYS90
D	AKG201
D	MG202
D	HOH2040
E	GLY27
E	MET28
E	THR29
E	GLU62
E	VAL64
E	ARG101
E	ARG103
E	HOH2031

site_id	BC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE AKG D 201

Chain	Residue
D	ARG9
D	PHE36
D	GLY37
D	ARG38
D	GLN39
D	LYS40
D	GLY41
D	LEU56
D	LYS58
D	ILE86
D	GLY87
D	ATP200
D	MG202
D	HOH2040

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 202

Chain	Residue
D	GLN39
D	GLY87
D	ATP200
D	AKG201

site_id	BC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ATP E 200

Chain	Residue
E	ILE7
E	GLY35
E	PHE36
E	GLY37
E	ARG38
E	GLN39
E	LYS58
E	ILE86
E	GLY87
E	ASP88
E	GLY89
E	LYS90
E	AKG201
E	MG202
E	HOH2035
E	HOH2036
E	HOH2038
F	GLY27
F	MET28
F	THR29
F	GLU62
F	VAL64
F	ARG101
F	ARG103

site_id	BC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE AKG E 201

Chain	Residue
E	ARG9
E	PHE36
E	GLY37
E	ARG38
E	GLN39
E	LYS40
E	GLY41
E	GLN42
E	LEU56
E	LYS58
E	ILE86
E	GLY87
E	ATP200
E	MG202
E	HOH2037
E	HOH2038

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 202

Chain	Residue
E	GLN39
E	GLY87
E	ATP200
E	AKG201

site_id	BC7
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ATP F 200

Chain	Residue
D	GLY27
D	MET28
D	THR29
D	GLU62
D	VAL64
D	ARG101
D	ARG103
F	ILE7
F	GLY35
F	PHE36
F	GLY37
F	ARG38
F	GLN39
F	ILE86
F	GLY87
F	ASP88
F	GLY89
F	LYS90
F	AKG201
F	MG202
F	HOH2036
F	HOH2037
F	HOH2038

site_id	BC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE AKG F 201

Chain	Residue
F	ARG9
F	GLY37
F	ARG38
F	GLN39
F	LYS40
F	GLY41
F	LEU56
F	LYS58
F	ILE86
F	GLY87
F	ATP200
F	MG202
F	HOH2038

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG F 202

Chain	Residue
F	GLN39
F	ATP200
F	AKG201

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
A	TYR46-TYR51

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

Chain	Residue	Details
A	THR83-VAL96

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Modified residue: {"description":"O-UMP-tyrosine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00675","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"7592328","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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