2AJ4

Crystal structure of Saccharomyces cerevisiae Galactokinase in complex with galactose and Mg:AMPPNP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000411	biological_process	positive regulation of transcription by galactose
A	0000435	biological_process	positive regulation of transcription from RNA polymerase II promoter by galactose
A	0004335	molecular_function	galactokinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005667	cellular_component	transcription regulator complex
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006012	biological_process	galactose metabolic process
A	0016301	molecular_function	kinase activity
A	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
A	0033499	biological_process	galactose catabolic process via UDP-galactose
A	0046835	biological_process	carbohydrate phosphorylation
B	0000411	biological_process	positive regulation of transcription by galactose
B	0000435	biological_process	positive regulation of transcription from RNA polymerase II promoter by galactose
B	0004335	molecular_function	galactokinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005667	cellular_component	transcription regulator complex
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006012	biological_process	galactose metabolic process
B	0016301	molecular_function	kinase activity
B	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
B	0033499	biological_process	galactose catabolic process via UDP-galactose
B	0046835	biological_process	carbohydrate phosphorylation

Functional Information from PROSITE/UniProt

site_id	PS00106
Number of Residues	12
Details	GALACTOKINASE Galactokinase signature. GRvNLIGEHiDY

Chain	Residue	Details
A	GLY52-TYR63

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site_id	PS00627
Number of Residues	12
Details	GHMP_KINASES_ATP GHMP kinases putative ATP-binding domain. VPtGsGLSSSAA

Chain	Residue	Details
A	VAL162-ALA173

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q9HHB6

Chain	Residue	Details
A	GLN218
B	GLN218

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site_id	SWS_FT_FI2
Number of Residues	28
Details	BINDING: BINDING => ECO:0000269|PubMed:16115868, ECO:0007744|PDB:2AJ4

Chain	Residue	Details
A	VAL54
A	GLN218
A	ASN265
A	LYS266
A	PHE267
A	ASN275
B	VAL54
B	HIS60
B	ILE61
B	TYR63
B	SER166
A	HIS60
B	LEU168
B	SER170
B	SER171
B	GLY214
B	GLN218
B	ASN265
B	LYS266
B	PHE267
B	ASN275
A	ILE61
A	TYR63
A	SER166
A	LEU168
A	SER170
A	SER171
A	GLY214

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site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Transition state stabilizer => ECO:0000250|UniProtKB:Q9HHB6

Chain	Residue	Details
A	VAL54
B	VAL54

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198

Chain	Residue	Details
A	PRO382
B	PRO382

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