1IG0

Crystal Structure of yeast Thiamin Pyrophosphokinase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004788	molecular_function	thiamine diphosphokinase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006772	biological_process	thiamine metabolic process
A	0009229	biological_process	thiamine diphosphate biosynthetic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0030975	molecular_function	thiamine binding
A	0042723	biological_process	thiamine-containing compound metabolic process
A	0044281	biological_process	small molecule metabolic process
B	0000166	molecular_function	nucleotide binding
B	0004788	molecular_function	thiamine diphosphokinase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006772	biological_process	thiamine metabolic process
B	0009229	biological_process	thiamine diphosphate biosynthetic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0030975	molecular_function	thiamine binding
B	0042723	biological_process	thiamine-containing compound metabolic process
B	0044281	biological_process	small molecule metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE VIB B 701

Chain	Residue
A	TRP270
B	THR125
B	HOH805
B	HOH971
A	VAL272
A	SER285
A	SER286
A	SER287
A	ASN288
B	GLN122
B	TYR123
B	SER124

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site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE VIB A 702

Chain	Residue
A	GLN122
A	TYR123
A	SER124
A	THR125
A	HOH784
A	HOH1011
B	TRP270
B	VAL272
B	SER285
B	SER286
B	SER287
B	ASN288

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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