Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3NM1

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	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	0016740	molecular_function	transferase activity
A	0046872	molecular_function	metal ion 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	0016740	molecular_function	transferase activity
B	0046872	molecular_function	metal ion 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	0016740	molecular_function	transferase activity
C	0046872	molecular_function	metal ion 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	0016740	molecular_function	transferase activity
D	0046872	molecular_function	metal ion 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	0016740	molecular_function	transferase activity
E	0046872	molecular_function	metal ion 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	0016740	molecular_function	transferase activity
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 3NM A 541

Chain	Residue
A	ARG45
A	IFP542
A	POP543
A	GLY138
A	THR139
A	THR143
A	THR145
A	LYS151
A	GLY181
A	VAL209
A	SER210

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE IFP A 542

Chain	Residue
A	TYR13
A	GLN43
A	HIS90
A	SER114
A	TYR134
A	GLY136
A	VAL177
A	ILE179
A	CYS207
A	3NM541
A	POP543

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE POP A 543

Chain	Residue
A	ARG45
A	LYS47
A	ASN75
A	ASP76
A	GLY92
A	ASP95
A	SER114
A	LYS146
A	3NM541
A	IFP542
A	MG544

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 3NM F 541

Chain	Residue
F	ARG45
F	GLY138
F	THR139
F	THR143
F	THR145
F	LYS146
F	LYS151
F	GLY180
F	GLY181
F	VAL209
F	SER210
F	IFP542

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE IFP F 542

Chain	Residue
F	TYR13
F	GLN43
F	HIS90
F	SER114
F	TYR134
F	GLY136
F	VAL177
F	ILE179
F	CYS207
F	3NM541
F	POP543

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE POP F 543

Chain	Residue
F	ARG45
F	LYS47
F	ASN75
F	ASP76
F	GLY92
F	ASP95
F	SER114
F	LYS146
F	IFP542
F	MG544

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 3NM E 541

Chain	Residue
E	ARG45
E	GLY138
E	THR139
E	THR143
E	THR145
E	LYS151
E	ILE179
E	GLY181
E	VAL209
E	SER210
E	IFP542
E	POP543

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE IFP E 542

Chain	Residue
E	TYR13
E	VAL15
E	GLN43
E	HIS90
E	SER114
E	TYR134
E	GLY136
E	VAL177
E	ILE179
E	CYS207
E	3NM541
E	POP543

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE POP E 543

Chain	Residue
E	MG544
E	ARG45
E	LYS47
E	ASN75
E	GLY92
E	ASP95
E	SER114
E	LYS146
E	3NM541
E	IFP542

site_id	BC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 3NM D 541

Chain	Residue
D	ARG45
D	THR139
D	THR143
D	THR145
D	LYS146
D	LYS151
D	GLY180
D	GLY181
D	VAL209
D	SER210
D	IFP542

site_id	BC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE IFP D 542

Chain	Residue
D	TYR13
D	VAL15
D	GLN43
D	HIS90
D	SER114
D	TYR134
D	GLY136
D	VAL177
D	ILE179
D	CYS207
D	3NM541
D	POP543

site_id	BC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE POP D 543

Chain	Residue
D	ARG45
D	LYS47
D	ASN75
D	ASP76
D	GLY92
D	ASP95
D	SER114
D	LYS146
D	IFP542
D	MG544

site_id	BC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 3NM C 541

Chain	Residue
C	ARG45
C	GLY138
C	THR139
C	THR143
C	THR145
C	LYS151
C	ILE179
C	GLY181
C	VAL209
C	SER210
C	IFP542
C	POP543

site_id	BC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE IFP C 542

Chain	Residue
C	TYR13
C	VAL15
C	GLN43
C	HIS90
C	SER114
C	TYR134
C	GLY136
C	VAL177
C	ILE179
C	CYS207
C	3NM541
C	POP543

site_id	BC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE POP C 543

Chain	Residue
C	ARG45
C	LYS47
C	ASN75
C	ASP76
C	GLY92
C	ASP95
C	SER114
C	LYS146
C	3NM541
C	IFP542
C	MG544

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 3NM B 541

Chain	Residue
B	ARG45
B	GLY138
B	THR139
B	THR143
B	THR145
B	LYS151
B	ILE179
B	GLY181
B	VAL209
B	SER210
B	IFP542

site_id	BC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE IFP B 542

Chain	Residue
B	TYR13
B	VAL15
B	GLN43
B	ASN75
B	HIS90
B	SER114
B	TYR134
B	GLY136
B	VAL177
B	ILE179
B	CYS207
B	3NM541
B	POP543

site_id	BC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE POP B 543

Chain	Residue
B	ARG45
B	LYS47
B	ASN75
B	GLY92
B	ASP95
B	SER114
B	LYS146
B	IFP542
B	MG544

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 544

Chain	Residue
A	ASP76
A	ASP95
A	POP543

site_id	CC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG F 544

Chain	Residue
F	ASP76
F	ASP95
F	POP543

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 544

Chain	Residue
E	LYS47
E	ASP76
E	ASP95
E	POP543

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 544

Chain	Residue
D	ASN75
D	ASP76
D	GLY92
D	ASP95
D	POP543

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 544

Chain	Residue
C	LYS47
C	ASP76
C	ASP95
C	POP543

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 544

Chain	Residue
B	LYS47
B	ASN75
B	ASP76
B	ASP95
B	POP543

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