Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4LRZ

Crystal Structure of the E.coli DhaR(N)-DhaL complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0004371	molecular_function	glycerone kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006071	biological_process	glycerol metabolic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
A	0019563	biological_process	glycerol catabolic process
A	0043531	molecular_function	ADP binding
A	0046835	biological_process	carbohydrate phosphorylation
A	0046872	molecular_function	metal ion binding
A	0047324	molecular_function	phosphoenolpyruvate-glycerone phosphotransferase activity
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0004371	molecular_function	glycerone kinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006071	biological_process	glycerol metabolic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
B	0019563	biological_process	glycerol catabolic process
B	0043531	molecular_function	ADP binding
B	0046835	biological_process	carbohydrate phosphorylation
B	0046872	molecular_function	metal ion binding
B	0047324	molecular_function	phosphoenolpyruvate-glycerone phosphotransferase activity
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0004371	molecular_function	glycerone kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006071	biological_process	glycerol metabolic process
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
C	0019563	biological_process	glycerol catabolic process
C	0043531	molecular_function	ADP binding
C	0046835	biological_process	carbohydrate phosphorylation
C	0046872	molecular_function	metal ion binding
C	0047324	molecular_function	phosphoenolpyruvate-glycerone phosphotransferase activity
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0004371	molecular_function	glycerone kinase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006071	biological_process	glycerol metabolic process
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
D	0019563	biological_process	glycerol catabolic process
D	0043531	molecular_function	ADP binding
D	0046835	biological_process	carbohydrate phosphorylation
D	0046872	molecular_function	metal ion binding
D	0047324	molecular_function	phosphoenolpyruvate-glycerone phosphotransferase activity
E	0006355	biological_process	regulation of DNA-templated transcription
F	0006355	biological_process	regulation of DNA-templated transcription
G	0006355	biological_process	regulation of DNA-templated transcription
H	0006355	biological_process	regulation of DNA-templated transcription

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ADP A 300

Chain	Residue
A	ASP30
A	ALA123
A	THR129
A	MET130
A	GLY177
A	ARG178
A	ASP191
A	PRO192
A	GLY193
A	MG301
A	MG302
A	ASP35
A	HOH401
A	HOH402
A	HOH408
A	HOH428
A	HOH456
A	HOH457
A	HOH458
A	ASP37
A	HIS38
A	GLY78
A	ALA79
A	SER80
A	LEU83
A	GLY121

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 301

Chain	Residue
A	ASP30
A	ASP35
A	ASP37
A	ADP300
A	HOH456

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 302

Chain	Residue
A	ASP35
A	ASP37
A	ADP300
A	HOH457
A	HOH458

site_id	AC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE ADP B 300

Chain	Residue
B	ASP30
B	ASP35
B	ASP37
B	HIS38
B	GLY78
B	ALA79
B	SER80
B	LEU83
B	GLY121
B	ALA123
B	THR129
B	MET130
B	GLY177
B	ARG178
B	ASP191
B	PRO192
B	GLY193
B	MG301
B	MG302
B	HOH401
B	HOH404
B	HOH411
B	HOH426
B	HOH429
B	HOH441
B	HOH444
H	HOH432

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 301

Chain	Residue
B	ASP30
B	ASP35
B	ASP37
B	ADP300
B	HOH441

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 302

Chain	Residue
B	ASP35
B	ASP37
B	ADP300
B	HOH429
B	HOH444

site_id	AC7
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ADP C 300

Chain	Residue
C	ASP30
C	ASP35
C	ASP37
C	HIS38
C	GLY78
C	ALA79
C	SER80
C	LEU83
C	GLY121
C	ALA123
C	THR129
C	MET130
C	GLY177
C	ARG178
C	ASP191
C	PRO192
C	GLY193
C	MG301
C	MG302
C	HOH403
C	HOH405
C	HOH406
C	HOH430
C	HOH449
C	HOH456
C	HOH457

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 301

Chain	Residue
C	ASP30
C	ASP35
C	ASP37
C	ADP300
C	HOH457

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 302

Chain	Residue
C	ASP35
C	ASP37
C	ADP300
C	HOH449
C	HOH456

site_id	BC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ADP D 300

Chain	Residue
D	ASP30
D	ASP35
D	ASP37
D	HIS38
D	GLY78
D	ALA79
D	SER80
D	LEU83
D	GLY121
D	ALA123
D	THR129
D	MET130
D	ARG178
D	ASP191
D	PRO192
D	GLY193
D	MG301
D	MG302
D	HOH402
D	HOH403
D	HOH416
D	HOH440
D	HOH445
D	HOH447
E	HOH458

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 301

Chain	Residue
D	ASP30
D	ASP35
D	ASP37
D	ADP300
D	HOH447

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 302

Chain	Residue
D	ASP35
D	ASP37
D	ADP300
D	HOH440
D	HOH446

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	800
Details	Domain: {"description":"DhaL","evidences":[{"source":"PROSITE-ProRule","id":"PRU00813","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16647083","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24440518","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BTD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LRZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16647083","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21209328","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24440518","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BTD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PNL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LRZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16647083","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21209328","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2BTD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	548
Details	Domain: {"description":"GAF","evidences":[{"source":"PubMed","id":"24440518","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	248
Details	Domain: {"description":"PAS","evidences":[{"source":"PubMed","id":"24440518","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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