Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1GLE

CATION PROMOTED ASSOCIATION (CPA) OF A REGULATORY AND TARGET PROTEIN IS CONTROLLED BY PHOSPHORYLATION

Functional Information from GO Data

Chain	GOid	namespace	contents
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0009401	biological_process	phosphoenolpyruvate-dependent sugar phosphotransferase system
F	0009898	cellular_component	cytoplasmic side of plasma membrane
F	0016020	cellular_component	membrane
F	0016301	molecular_function	kinase activity
F	0016740	molecular_function	transferase activity
F	0034763	biological_process	negative regulation of transmembrane transport
F	0043610	biological_process	regulation of carbohydrate utilization
F	0045912	biological_process	negative regulation of carbohydrate metabolic process
F	0046872	molecular_function	metal ion binding
F	1902344	biological_process	negative regulation of maltose transport
F	1902495	cellular_component	transmembrane transporter complex
F	1990154	cellular_component	enzyme IIA-maltose transporter complex
G	0000166	molecular_function	nucleotide binding
G	0003824	molecular_function	catalytic activity
G	0004370	molecular_function	glycerol kinase activity
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005829	cellular_component	cytosol
G	0005975	biological_process	carbohydrate metabolic process
G	0006071	biological_process	glycerol metabolic process
G	0006072	biological_process	glycerol-3-phosphate metabolic process
G	0006974	biological_process	DNA damage response
G	0008270	molecular_function	zinc ion binding
G	0016301	molecular_function	kinase activity
G	0016740	molecular_function	transferase activity
G	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
G	0019563	biological_process	glycerol catabolic process
G	0042802	molecular_function	identical protein binding
G	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN G 502

Chain	Residue
G	ARG17
G	G3H503
G	ADP504
G	ASP10

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN F 169

Chain	Residue
F	HIS75
F	HIS90
F	VAL96
F	HOH175
G	GLU478

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE G3H G 503

Chain	Residue
G	THR13
G	GLN82
G	ARG83
G	GLU84
G	TYR135
G	ASP245
G	THR267
G	PHE270
G	ZN502
G	ADP504

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ADP G 504

Chain	Residue
G	ARG17
G	GLY266
G	THR267
G	GLY310
G	ALA311
G	ALA326
G	GLY411
G	ALA412
G	ASN415
G	ZN502
G	G3H503

site_id	ZN1
Number of Residues	4
Details

Chain	Residue
F	HIS75
F	HIS90
G	GLU478
F	ZN169

site_id	ZN2
Number of Residues	4
Details

Chain	Residue
G	ASP10
G	G3H503
G	ADP504
G	ZN502

Functional Information from PROSITE/UniProt

site_id	PS00371
Number of Residues	13
Details	PTS_EIIA_TYPE_1_HIS PTS EIIA domains phosphorylation site signature 1. GveLFVHFGIdTV

Chain	Residue	Details
F	GLY84-VAL96

site_id	PS00445
Number of Residues	21
Details	FGGY_KINASES_2 FGGY family of carbohydrate kinases signature 2. GaIFGLtrgvnan.HIIRATLE

Chain	Residue	Details
G	GLY362-GLU382

site_id	PS00933
Number of Residues	13
Details	FGGY_KINASES_1 FGGY family of carbohydrate kinases signature 1. YfSgtKVKWILDH

Chain	Residue	Details
G	TYR135-HIS147

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	104
Details	Domain: {"description":"PTS EIIA type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00416","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Tele-phosphohistidine intermediate; for EIIA activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU00416","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2657735","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6383826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1961703","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9405042","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"2657735","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8170944","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9405042","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1961703","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Site: {"description":"Important for phospho-donor activity","evidences":[{"source":"PubMed","id":"2657735","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphohistidine; by HPr","evidences":[{"source":"PubMed","id":"2657735","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8170944","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GLC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10090737","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1BWF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10090737","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1GLJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8170944","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8430315","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9817843","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GLB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8430315","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9843423","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BO5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BOT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10090737","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1BWF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8170944","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8430315","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GLB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
F	HIS90
F	HIS75
F	GLY92
F	THR73

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)