4FOA

Crystal Structure of the Mtb ThyA in Complex with 5-fluoro-dUMP

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE UFP A 601

Chain	Residue
A	CYS146
A	TYR209
A	HOH759
A	HOH770
A	HOH851
B	ARG126
B	ARG127
A	HIS147
A	GLN165
A	ARG166
A	SER167
A	ASP169
A	GLY173
A	ASN177
A	HIS207

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site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE UFP B 301

Chain	Residue
A	ARG126
A	ARG127
B	CYS146
B	HIS147
B	GLN165
B	ARG166
B	SER167
B	ALA168
B	ASP169
B	GLY173
B	ASN177
B	HIS207
B	TYR209
B	HOH437

---

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE UFP C 301

Chain	Residue
C	ARG21
C	CYS146
C	HIS147
C	GLN165
C	ARG166
C	SER167
C	ASP169
C	GLY173
C	ASN177
C	HIS207
C	TYR209
C	HOH408
C	HOH421
D	ARG126
D	ARG127

---

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE UFP D 301

Chain	Residue
C	ARG126
C	ARG127
D	ARG21
D	CYS146
D	HIS147
D	GLN165
D	ARG166
D	SER167
D	ASP169
D	GLY173
D	ASN177
D	HIS207
D	TYR209
D	HOH414

---

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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
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	27
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	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":"4FOG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	4
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

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