Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2WVJ

Mutation of Thr163 to Ser in Human Thymidine Kinase Shifts the Specificity from Thymidine towards the Nucleoside Analogue Azidothymidine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004797	molecular_function	thymidine kinase activity
A	0005524	molecular_function	ATP binding
B	0004797	molecular_function	thymidine kinase activity
B	0005524	molecular_function	ATP binding
C	0004797	molecular_function	thymidine kinase activity
C	0005524	molecular_function	ATP binding
D	0004797	molecular_function	thymidine kinase activity
D	0005524	molecular_function	ATP binding
E	0004797	molecular_function	thymidine kinase activity
E	0005524	molecular_function	ATP binding
F	0004797	molecular_function	thymidine kinase activity
F	0005524	molecular_function	ATP binding
G	0004797	molecular_function	thymidine kinase activity
G	0005524	molecular_function	ATP binding
H	0004797	molecular_function	thymidine kinase activity
H	0005524	molecular_function	ATP binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	BINDING SITE FOR RESIDUE TTP A 1192

Chain	Residue
A	MET28
A	GLN100
A	PHE101
A	LEU124
A	THR127
A	PHE128
A	PHE133
A	SER163
A	VAL172
A	GLU173
A	VAL174
A	SER30
A	ILE175
A	GLY176
A	TYR181
A	HOH2116
A	HOH2117
A	HOH2118
A	HOH2119
A	GLY31
A	LYS32
A	SER33
A	ASP58
A	ARG60
A	ASP97
A	GLU98

site_id	AC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TTP B 1193

Chain	Residue
B	SER30
B	GLY31
B	LYS32
B	SER33
B	ASP58
B	ARG60
B	ASP97
B	GLU98
B	GLN100
B	PHE101
B	LEU124
B	THR127
B	PHE128
B	PHE133
B	SER163
B	VAL172
B	GLU173
B	VAL174
B	ILE175
B	GLY176
B	TYR181
B	HOH2135
B	HOH2136
B	HOH2137
B	HOH2139

site_id	AC3
Number of Residues	26
Details	BINDING SITE FOR RESIDUE TTP C 1192

Chain	Residue
C	MET28
C	SER30
C	GLY31
C	LYS32
C	SER33
C	ASP58
C	ARG60
C	ASP97
C	GLU98
C	GLN100
C	PHE101
C	LEU124
C	THR127
C	PHE128
C	PHE133
C	SER163
C	VAL172
C	GLU173
C	VAL174
C	ILE175
C	GLY176
C	TYR181
C	HOH2119
C	HOH2120
C	HOH2121
C	HOH2123

site_id	AC4
Number of Residues	28
Details	BINDING SITE FOR RESIDUE TTP D 1192

Chain	Residue
D	MG1193
D	HOH2056
D	HOH2135
D	HOH2136
D	HOH2137
D	HOH2138
D	MET28
D	PHE29
D	SER30
D	GLY31
D	LYS32
D	SER33
D	ASP58
D	ARG60
D	GLU98
D	PHE101
D	LEU124
D	THR127
D	PHE128
D	PHE133
D	SER163
D	ARG165
D	VAL172
D	GLU173
D	VAL174
D	ILE175
D	GLY176
D	TYR181

site_id	AC5
Number of Residues	26
Details	BINDING SITE FOR RESIDUE TTP E 1192

Chain	Residue
E	MET28
E	SER30
E	GLY31
E	LYS32
E	SER33
E	ASP58
E	ARG60
E	ASP97
E	GLU98
E	GLN100
E	PHE101
E	LEU124
E	THR127
E	PHE128
E	PHE133
E	SER163
E	ARG165
E	VAL172
E	GLU173
E	VAL174
E	ILE175
E	GLY176
E	TYR181
E	HOH2116
E	HOH2117
E	HOH2119

site_id	AC6
Number of Residues	24
Details	BINDING SITE FOR RESIDUE TTP F 1192

Chain	Residue
F	MET28
F	SER30
F	GLY31
F	LYS32
F	SER33
F	ASP58
F	ASP97
F	GLU98
F	GLN100
F	PHE101
F	LEU124
F	THR127
F	PHE128
F	PHE133
F	SER163
F	VAL172
F	GLU173
F	VAL174
F	ILE175
F	GLY176
F	TYR181
F	HOH2116
F	HOH2117
F	HOH2118

site_id	AC7
Number of Residues	28
Details	BINDING SITE FOR RESIDUE TTP G 1192

Chain	Residue
G	MET28
G	PHE29
G	SER30
G	GLY31
G	LYS32
G	SER33
G	ASP58
G	ARG60
G	GLU98
G	PHE101
G	LEU124
G	THR127
G	PHE128
G	PHE133
G	SER163
G	ARG165
G	VAL172
G	GLU173
G	VAL174
G	ILE175
G	GLY176
G	TYR181
G	MG1193
G	HOH2061
G	HOH2093
G	HOH2162
G	HOH2163
G	HOH2164

site_id	AC8
Number of Residues	27
Details	BINDING SITE FOR RESIDUE TTP H 1192

Chain	Residue
H	MET28
H	PHE29
H	SER30
H	GLY31
H	LYS32
H	SER33
H	ASP58
H	ARG60
H	GLU98
H	PHE101
H	LEU124
H	THR127
H	PHE128
H	PHE133
H	SER163
H	ARG165
H	VAL172
H	GLU173
H	VAL174
H	ILE175
H	GLY176
H	TYR181
H	MG1193
H	HOH2150
H	HOH2151
H	HOH2152
H	HOH2153

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 1193

Chain	Residue
D	SER33
D	TTP1192
D	HOH2009
D	HOH2056
D	HOH2057

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG G 1193

Chain	Residue
G	SER33
G	TTP1192
G	HOH2014
G	HOH2092

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG H 1193

Chain	Residue
H	SER33
H	TTP1192
H	HOH2013
H	HOH2077

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1193

Chain	Residue
A	CYS153
A	CYS156
A	CYS185
A	CYS188

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 1194

Chain	Residue
B	CYS153
B	CYS156
B	CYS185
B	CYS188

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 1193

Chain	Residue
C	CYS153
C	CYS156
C	CYS185
C	CYS188

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 1194

Chain	Residue
D	CYS153
D	CYS156
D	CYS185
D	CYS188

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 1193

Chain	Residue
E	CYS153
E	CYS156
E	CYS185
E	CYS188

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN F 1193

Chain	Residue
F	CYS153
F	CYS156
F	CYS185
F	CYS188

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN G 1194

Chain	Residue
G	CYS153
G	CYS156
G	CYS185
G	CYS188

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN H 1194

Chain	Residue
H	CYS153
H	CYS156
H	CYS185
H	CYS188

Functional Information from PROSITE/UniProt

site_id	PS00603
Number of Residues	14
Details	TK_CELLULAR_TYPE Thymidine kinase cellular-type signature. GgaDkYhSvCRlCY

Chain	Residue	Details
A	GLY176-TYR189

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	96
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15611477","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15733844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17407781","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22385435","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1W4R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XBT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ORV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WVJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15611477","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15733844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22385435","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1W4R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XBT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WVJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15733844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22385435","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1W4R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WVJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15611477","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15733844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17407781","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22385435","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1W4R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XBT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ORV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)