Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2XZW

STRUCTURE OF PII FROM SYNECHOCOCCUS ELONGATUS IN COMPLEX WITH 2- OXOGLUTARATE AT LOW 2-OG CONCENTRATIONS

Replaces: 2XUN

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
G	0000166	molecular_function	nucleotide binding
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005829	cellular_component	cytosol
G	0006351	biological_process	DNA-templated transcription
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	0006351	biological_process	DNA-templated transcription
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	0006351	biological_process	DNA-templated transcription
I	0006808	biological_process	regulation of nitrogen utilization
I	0030234	molecular_function	enzyme regulator activity
I	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ATP A 200

Chain	Residue
A	ILE7
A	ASP88
A	GLY89
A	LYS90
A	AKG201
A	MG202
A	HOH2025
A	HOH2026
B	GLY27
B	MET28
B	THR29
A	GLY35
B	GLU62
B	VAL64
B	ARG101
B	ARG103
B	HOH2037
A	PHE36
A	GLY37
A	ARG38
A	GLN39
A	LYS58
A	ILE86
A	GLY87

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AKG A 201

Chain	Residue
A	ARG9
A	GLY37
A	ARG38
A	GLN39
A	LYS40
A	GLY41
A	LEU56
A	LYS58
A	GLY87
A	ATP200
A	MG202
A	HOH2026

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	24
Details	BINDING SITE FOR RESIDUE ATP B 200

Chain	Residue
B	ILE7
B	GLY35
B	PHE36
B	ARG38
B	GLN39
B	LYS58
B	ILE86
B	GLY87
B	ASP88
B	GLY89
B	LYS90
B	AKG201
B	MG202
B	HOH2042
B	HOH2043
B	HOH2045
C	GLY27
C	MET28
C	THR29
C	GLU62
C	ILE63
C	VAL64
C	ARG101
C	ARG103

site_id	AC5
Number of Residues	15
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	LEU56
B	LYS58
B	ILE86
B	GLY87
B	ATP200
B	MG202
B	HOH2044
B	HOH2045

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	24
Details	BINDING SITE FOR RESIDUE ATP C 200

Chain	Residue
C	GLY89
C	LYS90
C	AKG201
C	MG202
C	HOH2040
C	HOH2041
A	GLY27
A	MET28
A	THR29
A	GLU62
A	VAL64
A	ARG101
A	ARG103
A	HOH2023
C	ILE7
C	GLY35
C	PHE36
C	GLY37
C	ARG38
C	GLN39
C	LYS58
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	HOH2040
C	HOH2042

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 202

Chain	Residue
C	GLN39
C	ATP200
C	AKG201

site_id	BC1
Number of Residues	21
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	HOH2039
D	HOH2040
E	GLY27
E	MET28
E	THR29
E	GLU62
E	ILE63
E	VAL64
E	ARG101
E	ARG103

site_id	BC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ATP E 200

Chain	Residue
E	ILE7
E	GLY35
E	PHE36
E	GLY37
E	ARG38
E	LYS58
E	ILE86
E	GLY87
E	ASP88
E	GLY89
E	LYS90
E	HOH2037
F	GLY27
F	MET28
F	THR29
F	GLU62
F	ILE63
F	VAL64
F	ARG101
F	ARG103
F	ILE112

site_id	BC3
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ATP F 200

Chain	Residue
D	GLY27
D	MET28
D	THR29
D	GLU62
D	ILE63
D	VAL64
D	ARG101
D	ARG103
F	ILE7
F	GLY35
F	PHE36
F	GLY37
F	ARG38
F	GLN39
F	LYS58
F	ILE86
F	GLY87
F	ASP88
F	GLY89
F	LYS90
F	AKG201
F	MG202
F	HOH2035
F	HOH2036
F	HOH2037

site_id	BC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE AKG F 201

Chain	Residue
F	ARG9
F	PHE36
F	GLY37
F	ARG38
F	GLN39
F	LYS40
F	GLY41
F	THR43
F	LEU56
F	LYS58
F	ILE86
F	GLY87
F	ATP200
F	MG202
F	HOH2037
F	HOH2038

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG F 202

Chain	Residue
F	GLN39
F	ATP200
F	AKG201

site_id	BC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ATP G 200

Chain	Residue
G	ILE7
G	GLY35
G	PHE36
G	GLY37
G	ARG38
G	GLN39
G	LYS58
G	GLY87
G	GLY89
G	LYS90
G	HOH2024
H	GLY27
H	MET28
H	THR29
H	GLU62
H	ILE63
H	VAL64
H	ARG101
H	ARG103

site_id	BC7
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ATP H 200

Chain	Residue
H	ILE7
H	GLY35
H	PHE36
H	ARG38
H	GLN39
H	ILE86
H	GLY87
H	ASP88
H	GLY89
H	LYS90
H	AKG201
H	MG202
H	HOH2026
H	HOH2027
I	VAL26
I	GLY27
I	MET28
I	THR29
I	GLU62
I	VAL64
I	ARG101
I	ARG103

site_id	BC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE AKG H 201

Chain	Residue
H	ARG9
H	GLY37
H	ARG38
H	GLN39
H	LYS40
H	GLY41
H	GLN42
H	LEU56
H	LYS58
H	ILE86
H	GLY87
H	ATP200
H	MG202
H	HOH2026

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

Chain	Residue
H	GLN39
H	ATP200
H	AKG201

site_id	CC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ATP I 200

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

site_id	CC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE AKG I 201

Chain	Residue
I	ARG9
I	GLY37
I	ARG38
I	GLN39
I	LYS40
I	GLY41
I	THR43
I	LEU56
I	LYS58
I	ILE86
I	GLY87
I	ATP200
I	MG202
I	HOH2038
I	HOH2039

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG I 202

Chain	Residue
I	GLN39
I	GLY87
I	ATP200
I	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	5
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)