2CGK

Crystal Structure of L-rhamnulose kinase from Escherichia coli in an open uncomplexed conformation.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004370	molecular_function	glycerol kinase activity
A	0005524	molecular_function	ATP binding
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0006071	biological_process	glycerol metabolic process
A	0008993	molecular_function	rhamnulokinase activity
A	0016301	molecular_function	kinase activity
A	0019299	biological_process	rhamnose metabolic process
A	0019301	biological_process	rhamnose catabolic process
A	0046835	biological_process	carbohydrate phosphorylation
B	0004370	molecular_function	glycerol kinase activity
B	0005524	molecular_function	ATP binding
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0006071	biological_process	glycerol metabolic process
B	0008993	molecular_function	rhamnulokinase activity
B	0016301	molecular_function	kinase activity
B	0019299	biological_process	rhamnose metabolic process
B	0019301	biological_process	rhamnose catabolic process
B	0046835	biological_process	carbohydrate phosphorylation

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01535, ECO:0000269|PubMed:16674975

Chain	Residue	Details
A	ASP237
B	ASP237

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site_id	SWS_FT_FI2
Number of Residues	14
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01535, ECO:0000269|PubMed:16674975

Chain	Residue	Details
A	HIS236
A	THR259
A	ASN296
A	GLN304
A	GLY402
B	ALA13
B	GLY83
B	HIS236
B	THR259
B	ASN296
B	GLN304
B	GLY402
A	ALA13
A	GLY83

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