1NN0

Crystal structure of human thymidylate kinase with ddTMP and ADP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004550	molecular_function	nucleoside diphosphate kinase activity
A	0004798	molecular_function	dTMP kinase activity
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0006227	biological_process	dUDP biosynthetic process
A	0006233	biological_process	dTDP biosynthetic process
A	0006235	biological_process	dTTP biosynthetic process
A	0009165	biological_process	nucleotide biosynthetic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0046105	biological_process	thymidine biosynthetic process
A	0071363	biological_process	cellular response to growth factor stimulus

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 401

Chain	Residue
A	SER20
A	ADP302
A	HOH505
A	HOH506
A	HOH507
A	HOH753

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 402

Chain	Residue
A	HOH761
A	HOH771
A	HOH771
A	HOH756
A	HOH756
A	HOH761

---

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE 2DT A 301

Chain	Residue
A	PHE42
A	LEU57
A	PHE72
A	ARG76
A	ARG97
A	GLY102
A	PHE105
A	TYR151
A	HOH505
A	HOH507
A	HOH513
A	HOH537
A	HOH607
A	HOH753
A	HOH757
A	HOH781
A	HOH797

---

site_id	AC4
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ADP A 302

Chain	Residue
A	ARG16
A	ALA17
A	GLY18
A	LYS19
A	SER20
A	THR21
A	ARG143
A	LYS182
A	SER183
A	ILE184
A	ARG192
A	MG401
A	HOH506
A	HOH507
A	HOH508
A	HOH522
A	HOH549
A	HOH556
A	HOH564
A	HOH645
A	HOH686
A	HOH754
A	HOH765

---

Functional Information from PROSITE/UniProt

site_id	PS01331
Number of Residues	13
Details	THYMIDYLATE_KINASE Thymidylate kinase signature. VVDRYafSGvAFT

Chain	Residue	Details
A	VAL94-THR106

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Region: {"description":"LID","evidences":[{"source":"PubMed","id":"12614151","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12614151","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NMX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NMY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NN0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NN3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12614151","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NMY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NMZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NN1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PDB","id":"1NMX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NMY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NN0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NN3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PDB","id":"1NMY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NMZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NN1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NN5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---