5COJ

Structure of Hydroxyethylthiazole kinase ThiM from Staphylococcus aureus in complex with native substrate 2-(4-methyl-1,3-thiazol-5-yl)ethanol.

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
E	0000287	molecular_function	magnesium ion binding
E	0004417	molecular_function	hydroxyethylthiazole kinase activity
E	0005524	molecular_function	ATP binding
E	0009228	biological_process	thiamine biosynthetic process
E	0009229	biological_process	thiamine diphosphate biosynthetic process
F	0000287	molecular_function	magnesium ion binding
F	0004417	molecular_function	hydroxyethylthiazole kinase activity
F	0005524	molecular_function	ATP binding
F	0009228	biological_process	thiamine biosynthetic process
F	0009229	biological_process	thiamine diphosphate biosynthetic process
H	0000287	molecular_function	magnesium ion binding
H	0004417	molecular_function	hydroxyethylthiazole kinase activity
H	0005524	molecular_function	ATP binding
H	0009228	biological_process	thiamine biosynthetic process
H	0009229	biological_process	thiamine diphosphate biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue TZE A 301

Chain	Residue
A	PRO37
A	ALA38
A	MET39
C	GLY61
C	THR186
C	CYS190

---

site_id	AC2
Number of Residues	6
Details	binding site for residue TZE A 302

Chain	Residue
A	CYS190
B	PRO37
B	MET39
A	GLY61
A	VAL90
A	THR186

---

site_id	AC3
Number of Residues	3
Details	binding site for residue MG A 303

Chain	Residue
A	ASP88
A	GLU120
A	HOH408

---

site_id	AC4
Number of Residues	3
Details	binding site for residue MG B 301

Chain	Residue
B	ASP88
B	GLY116
B	GLU120

---

site_id	AC5
Number of Residues	7
Details	binding site for residue TZE C 301

Chain	Residue
B	ASN19
B	GLY61
B	THR186
B	CYS190
C	PRO37
C	ALA38
C	MET39

---

site_id	AC6
Number of Residues	3
Details	binding site for residue MG C 302

Chain	Residue
C	ASP88
C	GLU120
C	HOH510

---

site_id	AC7
Number of Residues	6
Details	binding site for residue TZE E 301

Chain	Residue
E	GLY61
E	THR186
E	CYS190
E	HOH402
F	PRO37
F	MET39

---

site_id	AC8
Number of Residues	2
Details	binding site for residue MG E 302

Chain	Residue
E	ASP88
E	GLU120

---

site_id	AC9
Number of Residues	8
Details	binding site for residue TZE F 301

Chain	Residue
F	ASN19
F	VAL22
F	GLY61
F	THR186
F	CYS190
H	PRO37
H	ALA38
H	MET39

---

site_id	AD1
Number of Residues	6
Details	binding site for residue TZE H 301

Chain	Residue
E	PRO37
E	ALA38
E	MET39
H	GLY61
H	THR186
H	CYS190

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00228","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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