Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1XBT

Crystal Structure of Human Thymidine Kinase 1

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 1193

Chain	Residue
A	CYS153
A	CYS156
A	CYS185
A	CYS188

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 2193

Chain	Residue
B	CYS153
B	CYS156
B	CYS185
B	CYS188

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 3193

Chain	Residue
C	CYS156
C	CYS185
C	CYS188
C	CYS153

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 4193

Chain	Residue
D	CYS153
D	CYS156
D	CYS185
D	CYS188

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 5193

Chain	Residue
E	CYS153
E	CYS156
E	CYS185
E	CYS188

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN F 6193

Chain	Residue
F	CYS153
F	CYS156
F	CYS185
F	CYS188

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN G 7193

Chain	Residue
G	CYS153
G	CYS156
G	CYS185
G	CYS188

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN H 8193

Chain	Residue
H	CYS153
H	CYS156
H	CYS185
H	CYS188

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 1194

Chain	Residue
A	SER33
A	ARG60
A	TTP1195

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 2194

Chain	Residue
B	SER33
B	TTP2195

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 3194

Chain	Residue
C	SER33
C	TTP3195
C	HOH3215

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG D 4194

Chain	Residue
D	SER33
D	TTP4195
D	HOH4229

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG E 5194

Chain	Residue
E	SER33
E	TTP5195

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG F 6194

Chain	Residue
F	SER33
F	TTP6195

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG G 7194

Chain	Residue
G	SER33
G	TTP7195
G	HOH7228

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG H 8194

Chain	Residue
H	SER33
H	TTP8195
H	HOH8217

site_id	BC8
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TTP A 1195

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	ARG165
A	VAL172
A	GLU173
A	VAL174
A	ILE175
A	GLY176
A	TYR181
A	MG1194
A	HOH1202
A	HOH1214
A	HOH1218

site_id	BC9
Number of Residues	23
Details	BINDING SITE FOR RESIDUE TTP B 2195

Chain	Residue
B	MG2194
B	HOH2226
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	THR163
B	VAL172
B	GLU173
B	VAL174
B	ILE175
B	GLY176
B	TYR181

site_id	CC1
Number of Residues	26
Details	BINDING SITE FOR RESIDUE TTP C 3195

Chain	Residue
C	MET28
C	PHE29
C	SER30
C	GLY31
C	LYS32
C	SER33
C	ASP58
C	ARG60
C	GLU98
C	PHE101
C	LEU124
C	THR127
C	PHE128
C	PHE133
C	THR163
C	ARG165
C	VAL172
C	GLU173
C	VAL174
C	ILE175
C	GLY176
C	TYR181
C	MG3194
C	HOH3200
C	HOH3207
C	HOH3215

site_id	CC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TTP D 4195

Chain	Residue
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	ARG165
D	VAL172
D	GLU173
D	VAL174
D	GLY176
D	TYR181
D	MG4194
D	HOH4212
D	HOH4225
D	HOH4229
D	HOH4230

site_id	CC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE TTP E 5195

Chain	Residue
E	MET28
E	PHE29
E	SER30
E	GLY31
E	LYS32
E	SER33
E	ASP58
E	ARG60
E	GLU98
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	MG5194
E	HOH5214
E	HOH5215

site_id	CC4
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TTP F 6195

Chain	Residue
F	MET28
F	PHE29
F	SER30
F	GLY31
F	LYS32
F	SER33
F	ASP58
F	ARG60
F	PHE101
F	LEU124
F	THR127
F	PHE128
F	PHE133
F	THR163
F	ARG165
F	VAL172
F	GLU173
F	VAL174
F	ILE175
F	GLY176
F	TYR181
F	MG6194
F	HOH6210
F	HOH6219
F	HOH6220

site_id	CC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TTP G 7195

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	ARG165
G	VAL172
G	GLU173
G	VAL174
G	GLY176
G	TYR181
G	MG7194
G	HOH7202
G	HOH7214
G	HOH7216
G	HOH7228

site_id	CC6
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TTP H 8195

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	ARG165
H	VAL172
H	GLU173
H	VAL174
H	ILE175
H	GLY176
H	TYR181
H	MG8194
H	HOH8204
H	HOH8205
H	HOH8208

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

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
E	ASP58
E	VAL172
F	ASP58
F	VAL172
G	ASP58
G	VAL172
H	ASP58
H	VAL172
A	ASP58
A	VAL172
B	ASP58
B	VAL172
C	ASP58
C	VAL172
D	ASP58
D	VAL172

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

site_id	SWS_FT_FI6
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER2
B	SER2
C	SER2
D	SER2
E	SER2
F	SER2
G	SER2
H	SER2

site_id	SWS_FT_FI7
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:14697231, ECO:0000269\|PubMed:9575153, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER13
B	SER13
C	SER13
D	SER13
E	SER13
F	SER13
G	SER13
H	SER13

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