1ESJ

CRYSTAL STRUCTURE OF THIAZOLE KINASE MUTANT (C198S)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004417	molecular_function	hydroxyethylthiazole kinase activity
A	0005524	molecular_function	ATP binding
A	0009228	biological_process	thiamine biosynthetic process
A	0009229	biological_process	thiamine diphosphate biosynthetic process
B	0000287	molecular_function	magnesium ion binding
B	0004417	molecular_function	hydroxyethylthiazole kinase activity
B	0005524	molecular_function	ATP binding
B	0009228	biological_process	thiamine biosynthetic process
B	0009229	biological_process	thiamine diphosphate biosynthetic process
C	0000287	molecular_function	magnesium ion binding
C	0004417	molecular_function	hydroxyethylthiazole kinase activity
C	0005524	molecular_function	ATP binding
C	0009228	biological_process	thiamine biosynthetic process
C	0009229	biological_process	thiamine diphosphate biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 315

Chain	Residue
A	THR194
A	GLY195
A	ALA196
A	GLY197
A	SER198

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 325

Chain	Residue
C	HOH489
C	HOH554
C	HOH634
C	THR194
C	GLY195
C	GLY197
C	SER198

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00228","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10891066","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {}

Chain

Residue

Details

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