Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3HZG

Crystal structure of mycobacterium tuberculosis thymidylate synthase X bound with FAD

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004799	molecular_function	thymidylate synthase activity
A	0006231	biological_process	dTMP biosynthetic process
A	0006235	biological_process	dTTP biosynthetic process
A	0008168	molecular_function	methyltransferase activity
A	0009165	biological_process	nucleotide biosynthetic process
A	0016740	molecular_function	transferase activity
A	0032259	biological_process	methylation
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0050797	molecular_function	thymidylate synthase (FAD) activity
A	0070402	molecular_function	NADPH binding
B	0004799	molecular_function	thymidylate synthase activity
B	0006231	biological_process	dTMP biosynthetic process
B	0006235	biological_process	dTTP biosynthetic process
B	0008168	molecular_function	methyltransferase activity
B	0009165	biological_process	nucleotide biosynthetic process
B	0016740	molecular_function	transferase activity
B	0032259	biological_process	methylation
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0050797	molecular_function	thymidylate synthase (FAD) activity
B	0070402	molecular_function	NADPH binding
C	0004799	molecular_function	thymidylate synthase activity
C	0006231	biological_process	dTMP biosynthetic process
C	0006235	biological_process	dTTP biosynthetic process
C	0008168	molecular_function	methyltransferase activity
C	0009165	biological_process	nucleotide biosynthetic process
C	0016740	molecular_function	transferase activity
C	0032259	biological_process	methylation
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	0050797	molecular_function	thymidylate synthase (FAD) activity
C	0070402	molecular_function	NADPH binding
D	0004799	molecular_function	thymidylate synthase activity
D	0006231	biological_process	dTMP biosynthetic process
D	0006235	biological_process	dTTP biosynthetic process
D	0008168	molecular_function	methyltransferase activity
D	0009165	biological_process	nucleotide biosynthetic process
D	0016740	molecular_function	transferase activity
D	0032259	biological_process	methylation
D	0050660	molecular_function	flavin adenine dinucleotide binding
D	0050797	molecular_function	thymidylate synthase (FAD) activity
D	0070402	molecular_function	NADPH binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 A 1001

Chain	Residue
A	ARG87
D	PO41003
A	GLN103
A	SER105
A	GLN106
A	ARG172
A	HOH286
D	GLU92
D	HOH314
D	HOH315

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 1002

Chain	Residue
A	GLU92
A	ARG199
B	FAD501
D	PO41008

site_id	AC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE FAD A 501

Chain	Residue
A	CYS43
A	GLY68
A	HIS69
A	SER71
A	GLU74
A	HIS98
A	ASN188
A	ARG190
A	HOH271
A	HOH303
B	ARG95
B	HIS96
B	ARG97
B	HIS98
B	HIS194
B	ARG199
B	FAD501
B	PO41007
C	GLN103
C	TYR108

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 259

Chain	Residue
A	ARG87
A	SER88
A	HIS91
A	ASN177
D	ARG87
D	ASN177

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 B 1005

Chain	Residue
B	ARG87
B	SER105
B	GLN106
B	ARG172
B	HOH293
C	GLU92
C	HOH326
C	PO41004

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 B 1007

Chain	Residue
A	FAD501
B	GLU92
B	ARG95
B	ARG199
C	PO41006

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 B 1009

Chain	Residue
B	ARG87
B	SER88
B	HIS91
B	ASN177
C	ARG87
C	HIS91
C	ASN177

site_id	AC8
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FAD B 501

Chain	Residue
A	ARG95
A	HIS96
A	ARG97
A	HIS98
A	HIS194
A	ARG199
A	HOH267
A	FAD501
A	PO41002
B	CYS43
B	TYR44
B	GLY68
B	HIS69
B	SER71
B	GLU74
B	HIS98
B	ASN188
B	ARG190
B	HOH294
B	HOH297
B	HOH300
D	SER102
D	GLN103

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 C 1004

Chain	Residue
B	PO41005
C	GLU92
C	ARG95
C	ARG199
C	HOH326
C	FAD501

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 C 1006

Chain	Residue
B	GLU92
B	PO41007
C	ARG87
C	GLN103
C	SER105
C	GLN106
C	ARG172
C	HOH304

site_id	BC2
Number of Residues	27
Details	BINDING SITE FOR RESIDUE FAD C 501

Chain	Residue
B	GLN103
B	SER105
B	TYR108
C	ARG95
C	HIS96
C	ARG97
C	HIS98
C	HIS194
C	MET198
C	ARG199
C	GOL260
C	HOH264
C	HOH312
C	PO41004
D	CYS43
D	TYR44
D	VAL67
D	GLY68
D	HIS69
D	SER71
D	GLU74
D	HIS98
D	ASN188
D	ARG190
D	FAD501
B	SER100
B	SER102

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 259

Chain	Residue
C	PHE70
C	ARG190
D	FAD501

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 260

Chain	Residue
B	ARG107
B	TYR108
C	MET198
C	ARG199
C	HIS203
C	FAD501

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 D 1003

Chain	Residue
A	PO41001
D	GLU92
D	ARG95
D	ARG199
D	HOH314
D	HOH315
D	FAD501

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 D 1008

Chain	Residue
A	GLU92
A	PO41002
D	ARG87
D	SER105
D	GLN106
D	ARG172

site_id	BC7
Number of Residues	24
Details	BINDING SITE FOR RESIDUE FAD D 501

Chain	Residue
A	SER100
A	SER102
A	GLN103
A	TYR108
C	CYS43
C	GLY68
C	HIS69
C	SER71
C	GLU74
C	HIS98
C	ASN188
C	ARG190
C	GOL259
C	FAD501
D	ARG95
D	HIS96
D	ARG97
D	HIS98
D	HIS194
D	ARG199
D	HOH259
D	HOH296
D	HOH297
D	PO41003

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	904
Details	Domain: {"description":"ThyX","evidences":[{"source":"PROSITE-ProRule","id":"PRU00661","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	40
Details	Motif: {"description":"ThyX motif","evidences":[{"source":"HAMAP-Rule","id":"MF_01408","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"Involved in ionization of N3 of dUMP, leading to its activation","evidences":[{"source":"HAMAP-Rule","id":"MF_01408","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16139296","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2AF6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3GWC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HZG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	24
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"16139296","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2AF6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16139296","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2AF6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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