1F4B

CRYSTAL STRUCTURE OF ESCHERICHIA COLI THYMIDYLATE SYNTHASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003723	molecular_function	RNA binding
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	0006417	biological_process	regulation of translation
A	0008168	molecular_function	methyltransferase activity
A	0009165	biological_process	nucleotide biosynthetic process
A	0009314	biological_process	response to radiation
A	0016740	molecular_function	transferase activity
A	0016741	molecular_function	transferase activity, transferring one-carbon groups
A	0032259	biological_process	methylation
A	0042803	molecular_function	protein homodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 303

Chain	Residue
A	HIS51
A	LEU52
A	ARG53
A	GOL302
A	HOH424
A	HOH494
A	HOH496

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 304

Chain	Residue
A	HOH533
A	HOH547
A	LEU218
A	ARG222

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 305

Chain	Residue
A	GLU223
A	ARG225
A	HIS255
A	HOH504
A	HOH514

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 301

Chain	Residue
A	ARG126
A	ARG166
A	SER167
A	HOH431
A	HOH510

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 302

Chain	Residue
A	ILE56
A	PHE244
A	PHE247
A	GLU248
A	ILE249
A	SO4303
A	HOH312

---

Functional Information from PROSITE/UniProt

site_id	PS00091
Number of Residues	29
Details	THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriIvsaWNvgeldkma.....LaPCHaffQFyV

Chain	Residue	Details
A	ARG126-VAL154

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00008","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2223754","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8973201","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9416600","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	7
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"2223754","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8973201","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KCE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2TSC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8312270","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1TYS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"2223754","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8973201","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KCE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2TSC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1b02

Chain	Residue	Details
A	HIS207
A	GLU58
A	ASP169
A	SER167
A	CYS146
A	ASP205

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1b02

Chain	Residue	Details
A	SER180
A	ASN177
A	CYS146

---