1E9E

Mutant human thymidylate kinase (F105Y) complexed with dTMP 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	HOH2032
A	HOH2144
A	HOH2293
A	HOH2296

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

Chain	Residue
A	HOH2163
A	HOH2164
A	HOH2164
A	HOH2067
A	HOH2067
A	HOH2163

---

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE TMP A 301

Chain	Residue
A	PHE42
A	PRO43
A	ARG45
A	LEU57
A	PHE72
A	ARG76
A	ARG97
A	GLY102
A	TYR105
A	TYR151
A	HOH2144
A	HOH2288
A	HOH2289
A	HOH2290
A	HOH2291
A	HOH2292
A	HOH2293
A	HOH2294
A	HOH2295

---

site_id	AC4
Number of Residues	27
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	GLU196
A	MG401
A	HOH2144
A	HOH2293
A	HOH2296
A	HOH2297
A	HOH2298
A	HOH2299
A	HOH2300
A	HOH2301
A	HOH2302
A	HOH2303
A	HOH2305
A	HOH2306
A	HOH2307
A	HOH2308

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL94-THR106

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:12614151, ECO:0007744|PDB:1NMX, ECO:0007744|PDB:1NMY, ECO:0007744|PDB:1NN0, ECO:0007744|PDB:1NN3

Chain	Residue	Details
A	ARG16

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:12614151, ECO:0007744|PDB:1NMY, ECO:0007744|PDB:1NMZ, ECO:0007744|PDB:1NN1

Chain	Residue	Details
A	ARG97

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0007744|PDB:1NMX, ECO:0007744|PDB:1NMY, ECO:0007744|PDB:1NN0, ECO:0007744|PDB:1NN3

Chain	Residue	Details
A	LYS182

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0007744|PDB:1NMY, ECO:0007744|PDB:1NMZ, ECO:0007744|PDB:1NN1, ECO:0007744|PDB:1NN5

Chain	Residue	Details
A	ARG192

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330

Chain	Residue	Details
A	ALA2

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS169

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