Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3NL3

The Crystal Structure of Candida glabrata THI6, a Bifunctional Enzyme involved in Thiamin Biosyhthesis of Eukaryotes

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0004417	molecular_function	hydroxyethylthiazole kinase activity
A	0004789	molecular_function	thiamine-phosphate diphosphorylase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0009228	biological_process	thiamine biosynthetic process
A	0009229	biological_process	thiamine diphosphate biosynthetic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0004417	molecular_function	hydroxyethylthiazole kinase activity
B	0004789	molecular_function	thiamine-phosphate diphosphorylase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0009228	biological_process	thiamine biosynthetic process
B	0009229	biological_process	thiamine diphosphate biosynthetic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0004417	molecular_function	hydroxyethylthiazole kinase activity
C	0004789	molecular_function	thiamine-phosphate diphosphorylase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0009228	biological_process	thiamine biosynthetic process
C	0009229	biological_process	thiamine diphosphate biosynthetic process
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0004417	molecular_function	hydroxyethylthiazole kinase activity
D	0004789	molecular_function	thiamine-phosphate diphosphorylase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0009228	biological_process	thiamine biosynthetic process
D	0009229	biological_process	thiamine diphosphate biosynthetic process
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0046872	molecular_function	metal ion binding
E	0000166	molecular_function	nucleotide binding
E	0000287	molecular_function	magnesium ion binding
E	0004417	molecular_function	hydroxyethylthiazole kinase activity
E	0004789	molecular_function	thiamine-phosphate diphosphorylase activity
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0009228	biological_process	thiamine biosynthetic process
E	0009229	biological_process	thiamine diphosphate biosynthetic process
E	0016301	molecular_function	kinase activity
E	0016740	molecular_function	transferase activity
E	0046872	molecular_function	metal ion binding
F	0000166	molecular_function	nucleotide binding
F	0000287	molecular_function	magnesium ion binding
F	0004417	molecular_function	hydroxyethylthiazole kinase activity
F	0004789	molecular_function	thiamine-phosphate diphosphorylase activity
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0009228	biological_process	thiamine biosynthetic process
F	0009229	biological_process	thiamine diphosphate biosynthetic process
F	0016301	molecular_function	kinase activity
F	0016740	molecular_function	transferase activity
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE TPS A 2001

Chain	Residue
A	TYR13
A	GLY181
A	VAL209
A	SER210
A	GLN43
A	ARG45
A	HIS90
A	SER114
A	TYR134
A	THR143
A	THR145
A	ILE179

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TPS F 2002

Chain	Residue
F	GLN43
F	HIS90
F	SER114
F	THR143
F	THR145
F	ILE179
F	GLY181
F	VAL209
F	SER210

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TPS D 2003

Chain	Residue
D	GLN43
D	ARG45
D	HIS90
D	SER114
D	GLY136
D	THR143
D	THR145
D	ILE179
D	GLY181
D	VAL209
D	SER210

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE TPS C 2004

Chain	Residue
C	TYR13
C	GLN43
C	HIS90
C	SER114
C	THR139
C	THR143
C	THR145
C	ILE179
C	GLY180
C	GLY181
C	VAL209
C	SER210

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE TPS B 2005

Chain	Residue
B	TYR13
B	GLN43
B	ARG45
B	HIS90
B	SER114
B	GLY136
B	THR143
B	THR145
B	ILE179
B	GLY181
B	VAL208
B	VAL209
B	SER210

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TPS E 2006

Chain	Residue
E	GLN43
E	HIS90
E	SER114
E	THR143
E	THR145
E	ILE179
E	GLY181
E	VAL209
E	SER210

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 541

Chain	Residue
A	THR51
C	ASP76
C	ASP95

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 541

Chain	Residue
A	ASP76
A	ASP95
C	THR51

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 542

Chain	Residue
A	LEU241
A	THR243
A	ASP424
A	THR426
A	ILE427
A	GLU428

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG F 541

Chain	Residue
B	THR51
F	ASP76
F	ASP95

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG D 541

Chain	Residue
D	ASP76
D	ASP95
E	THR51

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 542

Chain	Residue
D	ALA49
D	ASP50
D	THR51
E	ASP76
E	ASP95

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 543

Chain	Residue
A	ASP340
A	PRO341
A	GLU372

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG F 542

Chain	Residue
F	ASP340
F	PRO341
F	GLU372

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG D 543

Chain	Residue
D	ASP340
D	PRO341
D	GLU372

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 542

Chain	Residue
C	PRO341
C	GLU372
C	ASP340

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG B 541

Chain	Residue
B	ASP340
B	PRO341
B	GLU372

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG E 541

Chain	Residue
E	ASP340
E	PRO341
E	GLU372

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)