Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1W4R

Structure of a type II thymidine kinase with bound dTTP

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	4
Details	BINDING SITE FOR RESIDUE ZN A 400

Chain	Residue
A	CYS153
A	CYS156
A	CYS185
A	CYS188

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 400

Chain	Residue
B	CYS153
B	CYS156
B	CYS185
B	CYS188

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 400

Chain	Residue
C	CYS156
C	CYS185
C	CYS188
C	CYS153

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 400

Chain	Residue
D	CYS153
D	CYS156
D	CYS185
D	CYS188

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 400

Chain	Residue
E	CYS153
E	CYS156
E	CYS185
E	CYS188

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN F 400

Chain	Residue
F	CYS153
F	CYS156
F	CYS185
F	CYS188

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN G 400

Chain	Residue
G	CYS153
G	CYS156
G	CYS185
G	CYS188

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN H 400

Chain	Residue
H	CYS153
H	CYS156
H	CYS185
H	CYS188

site_id	AC9
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TTP A 300

Chain	Residue
A	MET28
A	PHE29
A	SER30
A	GLY31
A	LYS32
A	SER33
A	ASP58
A	ARG60
A	GLU98
A	PHE101
A	LEU124
A	THR127
A	PHE128
A	PHE133
A	VAL172
A	GLU173
A	VAL174
A	ILE175
A	GLY176
A	TYR181
A	HOH2104
A	HOH2105
A	HOH2108
A	HOH2109
A	HOH2110

site_id	BC1
Number of Residues	30
Details	BINDING SITE FOR RESIDUE TTP B 300

Chain	Residue
B	MET28
B	PHE29
B	SER30
B	GLY31
B	LYS32
B	SER33
B	ASP58
B	ARG60
B	GLU98
B	PHE101
B	LEU124
B	THR127
B	PHE128
B	PHE133
B	ARG165
B	VAL172
B	GLU173
B	VAL174
B	ILE175
B	GLY176
B	TYR181
B	HOH2034
B	HOH2100
B	HOH2102
B	HOH2103
B	HOH2104
B	HOH2105
B	HOH2106
B	HOH2107
B	HOH2108

site_id	BC2
Number of Residues	27
Details	BINDING SITE FOR RESIDUE TTP C 300

Chain	Residue
C	THR127
C	PHE128
C	PHE133
C	ARG165
C	VAL172
C	GLU173
C	VAL174
C	ILE175
C	GLY176
C	TYR181
C	HOH2080
C	HOH2081
C	HOH2083
C	HOH2084
C	HOH2085
C	PRO27
C	MET28
C	PHE29
C	SER30
C	GLY31
C	LYS32
C	SER33
C	ASP58
C	ARG60
C	GLU98
C	PHE101
C	LEU124

site_id	BC3
Number of Residues	28
Details	BINDING SITE FOR RESIDUE TTP D 300

Chain	Residue
D	MET28
D	SER30
D	GLY31
D	LYS32
D	SER33
D	ASP58
D	ARG60
D	ASP97
D	GLU98
D	GLN100
D	PHE101
D	LEU124
D	THR127
D	PHE128
D	PHE133
D	VAL172
D	GLU173
D	VAL174
D	ILE175
D	GLY176
D	TYR181
D	HOH2088
D	HOH2089
D	HOH2090
D	HOH2092
D	HOH2093
D	HOH2094
D	HOH2095

site_id	BC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE TTP E 300

Chain	Residue
E	MET28
E	GLY31
E	LYS32
E	SER33
E	ASP58
E	ASP97
E	GLU98
E	GLN100
E	PHE101
E	LEU124
E	THR127
E	PHE128
E	PHE133
E	ARG165
E	VAL172
E	GLU173
E	VAL174
E	ILE175
E	GLY176
E	TYR181
E	HOH2075
E	HOH2076
E	HOH2077
E	HOH2078
E	HOH2079
E	HOH2080
E	HOH2081

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE DTU E 1193

Chain	Residue
B	ARG82
B	ASP104
B	GLU107
B	ALA111
E	GLU110
E	ALA111
E	ASN114
E	HOH2082
E	HOH2083

site_id	BC6
Number of Residues	29
Details	BINDING SITE FOR RESIDUE TTP F 300

Chain	Residue
F	MET28
F	SER30
F	GLY31
F	LYS32
F	SER33
F	ASP58
F	ARG60
F	ASP97
F	GLU98
F	GLN100
F	PHE101
F	LEU124
F	THR127
F	PHE128
F	PHE133
F	VAL172
F	GLU173
F	VAL174
F	ILE175
F	GLY176
F	TYR181
F	HOH2109
F	HOH2110
F	HOH2111
F	HOH2112
F	HOH2113
F	HOH2115
F	HOH2116
F	HOH2117

site_id	BC7
Number of Residues	28
Details	BINDING SITE FOR RESIDUE TTP G 300

Chain	Residue
G	MET28
G	SER30
G	GLY31
G	LYS32
G	SER33
G	ASP58
G	ARG60
G	ASP97
G	GLU98
G	GLN100
G	PHE101
G	LEU124
G	THR127
G	PHE128
G	PHE133
G	VAL172
G	GLU173
G	VAL174
G	ILE175
G	GLY176
G	TYR181
G	HOH2100
G	HOH2101
G	HOH2102
G	HOH2103
G	HOH2106
G	HOH2107
G	HOH2108

site_id	BC8
Number of Residues	29
Details	BINDING SITE FOR RESIDUE TTP H 300

Chain	Residue
H	MET28
H	GLY31
H	LYS32
H	SER33
H	ASP58
H	ARG60
H	ASP97
H	GLU98
H	GLN100
H	PHE101
H	LEU124
H	THR127
H	PHE128
H	PHE133
H	ARG165
H	VAL172
H	GLU173
H	VAL174
H	ILE175
H	GLY176
H	TYR181
H	HOH2081
H	HOH2082
H	HOH2083
H	HOH2084
H	HOH2085
H	HOH2086
H	HOH2087
H	HOH2088

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	ACT_SITE: Proton acceptor => ECO:0000255

Chain	Residue	Details
A	GLU98
B	GLU98
C	GLU98
D	GLU98
E	GLU98
F	GLU98
G	GLU98
H	GLU98

site_id	SWS_FT_FI2
Number of Residues	48
Details	BINDING: BINDING => ECO:0000269\|PubMed:15611477, ECO:0000269\|PubMed:15733844, ECO:0000269\|PubMed:17407781, ECO:0000269\|PubMed:22385435, ECO:0007744\|PDB:1W4R, ECO:0007744\|PDB:1XBT, ECO:0007744\|PDB:2ORV, ECO:0007744\|PDB:2WVJ

Chain	Residue	Details
A	GLY26
B	CYS156
B	CYS185
B	CYS188
C	GLY26
C	PHE128
C	CYS153
C	CYS156
C	CYS185
C	CYS188
D	GLY26
A	PHE128
D	PHE128
D	CYS153
D	CYS156
D	CYS185
D	CYS188
E	GLY26
E	PHE128
E	CYS153
E	CYS156
E	CYS185
A	CYS153
E	CYS188
F	GLY26
F	PHE128
F	CYS153
F	CYS156
F	CYS185
F	CYS188
G	GLY26
G	PHE128
G	CYS153
A	CYS156
G	CYS156
G	CYS185
G	CYS188
H	GLY26
H	PHE128
H	CYS153
H	CYS156
H	CYS185
H	CYS188
A	CYS185
A	CYS188
B	GLY26
B	PHE128
B	CYS153

site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:15611477, ECO:0000269\|PubMed:15733844, ECO:0000269\|PubMed:22385435, ECO:0007744\|PDB:1W4R, ECO:0007744\|PDB:1XBT, ECO:0007744\|PDB:2WVJ

Chain	Residue	Details
A	ASP58
E	VAL172
F	ASP58
F	VAL172
G	ASP58
G	VAL172
H	ASP58
H	VAL172
A	VAL172
B	ASP58
B	VAL172
C	ASP58
C	VAL172
D	ASP58
D	VAL172
E	ASP58

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:15733844, ECO:0000269\|PubMed:22385435, ECO:0007744\|PDB:1W4R, ECO:0007744\|PDB:2WVJ

Chain	Residue	Details
A	ASP97
B	ASP97
C	ASP97
D	ASP97
E	ASP97
F	ASP97
G	ASP97
H	ASP97

site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:15611477, ECO:0000269\|PubMed:15733844, ECO:0000269\|PubMed:17407781, ECO:0000269\|PubMed:22385435, ECO:0007744\|PDB:1W4R, ECO:0007744\|PDB:1XBT, ECO:0007744\|PDB:2ORV

Chain	Residue	Details
A	TYR181
B	TYR181
C	TYR181
D	TYR181
E	TYR181
F	TYR181
G	TYR181
H	TYR181

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