4FOX

Crystal Structure of Mtb ThyA in complex with dUMP and Raltitrexed

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004799	molecular_function	thymidylate synthase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
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	0016741	molecular_function	transferase activity, transferring one-carbon groups
A	0032259	biological_process	methylation
A	0046079	biological_process	dUMP catabolic process
A	0046677	biological_process	response to antibiotic
B	0004799	molecular_function	thymidylate synthase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
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	0016741	molecular_function	transferase activity, transferring one-carbon groups
B	0032259	biological_process	methylation
B	0046079	biological_process	dUMP catabolic process
B	0046677	biological_process	response to antibiotic
C	0004799	molecular_function	thymidylate synthase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
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	0016741	molecular_function	transferase activity, transferring one-carbon groups
C	0032259	biological_process	methylation
C	0046079	biological_process	dUMP catabolic process
C	0046677	biological_process	response to antibiotic
D	0004799	molecular_function	thymidylate synthase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
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	0016741	molecular_function	transferase activity, transferring one-carbon groups
D	0032259	biological_process	methylation
D	0046079	biological_process	dUMP catabolic process
D	0046677	biological_process	response to antibiotic
E	0004799	molecular_function	thymidylate synthase activity
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006231	biological_process	dTMP biosynthetic process
E	0006235	biological_process	dTTP biosynthetic process
E	0008168	molecular_function	methyltransferase activity
E	0009165	biological_process	nucleotide biosynthetic process
E	0016740	molecular_function	transferase activity
E	0016741	molecular_function	transferase activity, transferring one-carbon groups
E	0032259	biological_process	methylation
E	0046079	biological_process	dUMP catabolic process
E	0046677	biological_process	response to antibiotic
F	0004799	molecular_function	thymidylate synthase activity
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006231	biological_process	dTMP biosynthetic process
F	0006235	biological_process	dTTP biosynthetic process
F	0008168	molecular_function	methyltransferase activity
F	0009165	biological_process	nucleotide biosynthetic process
F	0016740	molecular_function	transferase activity
F	0016741	molecular_function	transferase activity, transferring one-carbon groups
F	0032259	biological_process	methylation
F	0046079	biological_process	dUMP catabolic process
F	0046677	biological_process	response to antibiotic
G	0004799	molecular_function	thymidylate synthase activity
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0006231	biological_process	dTMP biosynthetic process
G	0006235	biological_process	dTTP biosynthetic process
G	0008168	molecular_function	methyltransferase activity
G	0009165	biological_process	nucleotide biosynthetic process
G	0016740	molecular_function	transferase activity
G	0016741	molecular_function	transferase activity, transferring one-carbon groups
G	0032259	biological_process	methylation
G	0046079	biological_process	dUMP catabolic process
G	0046677	biological_process	response to antibiotic
H	0004799	molecular_function	thymidylate synthase activity
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0006231	biological_process	dTMP biosynthetic process
H	0006235	biological_process	dTTP biosynthetic process
H	0008168	molecular_function	methyltransferase activity
H	0009165	biological_process	nucleotide biosynthetic process
H	0016740	molecular_function	transferase activity
H	0016741	molecular_function	transferase activity, transferring one-carbon groups
H	0032259	biological_process	methylation
H	0046079	biological_process	dUMP catabolic process
H	0046677	biological_process	response to antibiotic

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE D16 A 301

Chain	Residue
A	HIS51
A	GLY173
A	PHE176
A	TYR209
A	UMP302
A	HOH409
A	HOH436
A	SER54
A	GLU58
A	ILE79
A	TRP80
A	TRP83
A	LEU143
A	ASP169
A	LEU172

---

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE UMP A 302

Chain	Residue
A	ARG21
A	CYS146
A	HIS147
A	GLN165
A	ARG166
A	SER167
A	ALA168
A	ASP169
A	ASN177
A	HIS207
A	TYR209
A	D16301
A	HOH410
A	HOH468
B	ARG126
B	ARG127

---

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE UMP B 301

Chain	Residue
A	ARG126
A	ARG127
B	ARG21
B	CYS146
B	HIS147
B	GLN165
B	ARG166
B	SER167
B	ALA168
B	ASP169
B	ASN177
B	HIS207
B	TYR209
B	D16302
B	HOH427

---

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE D16 B 302

Chain	Residue
B	HIS51
B	SER54
B	GLU58
B	ILE79
B	TRP80
B	TRP83
B	LEU143
B	ASP169
B	LEU172
B	GLY173
B	PHE176
B	TYR209
B	UMP301
B	HOH410
B	HOH425

---

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE D16 C 301

Chain	Residue
C	HIS51
C	SER54
C	GLU58
C	TRP80
C	TRP83
C	ASP169
C	LEU172
C	GLY173
C	PHE176
C	TYR209
C	UMP302

---

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE UMP C 302

Chain	Residue
C	ARG21
C	CYS146
C	HIS147
C	GLN165
C	ARG166
C	SER167
C	ALA168
C	ASP169
C	ASN177
C	HIS207
C	TYR209
C	D16301
C	HOH409
D	ARG126
D	ARG127

---

site_id	AC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE D16 D 301

Chain	Residue
D	UMP302
D	HOH402
D	HOH414
D	HOH416
D	HOH460
D	HOH462
D	HOH466
D	HIS51
D	SER54
D	GLU58
D	ILE79
D	TRP80
D	TRP83
D	ASP169
D	LEU172
D	GLY173
D	PHE176
D	TYR209
D	ALA262

---

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE UMP D 302

Chain	Residue
C	ARG126
C	ARG127
D	ARG21
D	CYS146
D	HIS147
D	GLN165
D	ARG166
D	SER167
D	ALA168
D	ASP169
D	GLY173
D	ASN177
D	HIS207
D	TYR209
D	D16301
D	HOH402

---

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE D16 E 301

Chain	Residue
E	HIS51
E	GLU58
E	ILE79
E	TRP80
E	TRP83
E	ASP169
E	LEU172
E	GLY173
E	PHE176
E	TYR209
E	UMP302
E	HOH415

---

site_id	BC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE UMP E 302

Chain	Residue
E	ARG21
E	CYS146
E	HIS147
E	GLN165
E	ARG166
E	SER167
E	ALA168
E	ASP169
E	ASN177
E	HIS207
E	TYR209
E	D16301
E	HOH415
F	ARG126
F	ARG127

---

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE D16 F 301

Chain	Residue
F	HIS51
F	GLU58
F	TRP80
F	TRP83
F	ASP169
F	LEU172
F	GLY173
F	PHE176
F	TYR209
F	UMP302

---

site_id	BC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE UMP F 302

Chain	Residue
E	ARG126
E	ARG127
F	ARG21
F	CYS146
F	HIS147
F	GLN165
F	ARG166
F	SER167
F	ALA168
F	ASP169
F	ASN177
F	HIS207
F	TYR209
F	D16301
F	HOH407

---

site_id	BC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE D16 G 301

Chain	Residue
G	HIS51
G	SER54
G	GLU58
G	ILE79
G	TRP80
G	TRP83
G	LEU143
G	ASP169
G	LEU172
G	GLY173
G	PHE176
G	TYR209
G	UMP302
G	HOH409

---

site_id	BC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE UMP G 302

Chain	Residue
G	ARG21
G	CYS146
G	HIS147
G	GLN165
G	ARG166
G	SER167
G	ALA168
G	ASP169
G	ASN177
G	HIS207
G	TYR209
G	D16301
H	ARG126
H	ARG127

---

site_id	BC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE D16 H 301

Chain	Residue
H	HIS51
H	SER54
H	GLU58
H	ILE79
H	TRP80
H	TRP83
H	ASP169
H	LEU172
H	GLY173
H	PHE176
H	TYR209
H	UMP302

---

site_id	BC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE UMP H 302

Chain	Residue
G	ARG126
G	ARG127
H	ARG21
H	TYR94
H	CYS146
H	HIS147
H	GLN165
H	ARG166
H	SER167
H	ALA168
H	ASP169
H	ASN177
H	HIS207
H	TYR209
H	D16301

---

Functional Information from PROSITE/UniProt

site_id	PS00091
Number of Residues	29
Details	THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriIvsaWNvgeierma.....LpPCHaffQFyV

Chain	Residue	Details
A	ARG126-VAL154

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00008","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	56
Details	Binding site: {"description":"in other chain","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of binary and ternary complexes of thymidylate synthase (ThyA) from Mycobacterium tuberculosis: insights into the selectivity and mode of inhibition.","authors":["Reddy M.C.M.","Bruning J.B.","Harshbarger W.","Sacchettini J.C."]}},{"source":"PDB","id":"3QJ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FOX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FQS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	17
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of binary and ternary complexes of thymidylate synthase (ThyA) from Mycobacterium tuberculosis: insights into the selectivity and mode of inhibition.","authors":["Reddy M.C.M.","Bruning J.B.","Harshbarger W.","Sacchettini J.C."]}},{"source":"PDB","id":"4FOG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of binary and ternary complexes of thymidylate synthase (ThyA) from Mycobacterium tuberculosis: insights into the selectivity and mode of inhibition.","authors":["Reddy M.C.M.","Bruning J.B.","Harshbarger W.","Sacchettini J.C."]}},{"source":"PDB","id":"3QJ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FOX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FQS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---