5CGE

Structure of Hydroxyethylthiazole Kinase ThiM from Staphylococcus aureus in complex with substrate analog 2-(2-methyl-1H-imidazole-1-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
D	0000287	molecular_function	magnesium ion binding
D	0004417	molecular_function	hydroxyethylthiazole kinase activity
D	0005524	molecular_function	ATP binding
D	0009228	biological_process	thiamine biosynthetic process
D	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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue 51F A 301

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

---

site_id	AC2
Number of Residues	3
Details	binding site for residue MG A 302

Chain	Residue
A	HOH402
A	HOH426
A	HOH459

---

site_id	AC3
Number of Residues	7
Details	binding site for residue 51F B 301

Chain	Residue
A	ASN19
A	GLY61
A	THR186
A	CYS190
A	HOH470
B	PRO37
B	MET39

---

site_id	AC4
Number of Residues	2
Details	binding site for residue MG B 302

Chain	Residue
B	HOH406
B	HOH484

---

site_id	AC5
Number of Residues	6
Details	binding site for residue 51F C 301

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

---

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

Chain	Residue
C	ASP88
C	GLY116
C	GLU120

---

site_id	AC7
Number of Residues	5
Details	binding site for residue MG C 303

Chain	Residue
C	LEU57
C	ASN59
C	ASP88
C	CYS190
C	GLY193

---

site_id	AC8
Number of Residues	6
Details	binding site for residue 51F E 301

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

---

site_id	AC9
Number of Residues	3
Details	binding site for residue MG E 302

Chain	Residue
E	ASP88
E	GLU120
E	HOH452

---

site_id	AD1
Number of Residues	6
Details	binding site for residue 51F D 301

Chain	Residue
D	PRO37
D	MET39
E	GLY61
E	VAL90
E	THR186
E	CYS190

---

site_id	AD2
Number of Residues	5
Details	binding site for residue 51F D 302

Chain	Residue
D	GLY61
D	THR186
D	CYS190
F	PRO37
F	MET39

---

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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