Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6N55

Crystal structure of human uridine-cytidine kinase 2 complexed with 2'-azidouridine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004849	molecular_function	uridine kinase activity
A	0005524	molecular_function	ATP binding
A	0005575	cellular_component	cellular_component
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0009224	biological_process	CMP biosynthetic process
A	0016301	molecular_function	kinase activity
A	0042802	molecular_function	identical protein binding
A	0043771	molecular_function	cytidine kinase activity
A	0044206	biological_process	UMP salvage
A	0044211	biological_process	CTP salvage
B	0004849	molecular_function	uridine kinase activity
B	0005524	molecular_function	ATP binding
B	0005575	cellular_component	cellular_component
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0009224	biological_process	CMP biosynthetic process
B	0016301	molecular_function	kinase activity
B	0042802	molecular_function	identical protein binding
B	0043771	molecular_function	cytidine kinase activity
B	0044206	biological_process	UMP salvage
B	0044211	biological_process	CTP salvage
C	0004849	molecular_function	uridine kinase activity
C	0005524	molecular_function	ATP binding
C	0005575	cellular_component	cellular_component
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0009224	biological_process	CMP biosynthetic process
C	0016301	molecular_function	kinase activity
C	0042802	molecular_function	identical protein binding
C	0043771	molecular_function	cytidine kinase activity
C	0044206	biological_process	UMP salvage
C	0044211	biological_process	CTP salvage
D	0004849	molecular_function	uridine kinase activity
D	0005524	molecular_function	ATP binding
D	0005575	cellular_component	cellular_component
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0009224	biological_process	CMP biosynthetic process
D	0016301	molecular_function	kinase activity
D	0042802	molecular_function	identical protein binding
D	0043771	molecular_function	cytidine kinase activity
D	0044206	biological_process	UMP salvage
D	0044211	biological_process	CTP salvage
E	0004849	molecular_function	uridine kinase activity
E	0005524	molecular_function	ATP binding
E	0005575	cellular_component	cellular_component
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0009224	biological_process	CMP biosynthetic process
E	0016301	molecular_function	kinase activity
E	0042802	molecular_function	identical protein binding
E	0043771	molecular_function	cytidine kinase activity
E	0044206	biological_process	UMP salvage
E	0044211	biological_process	CTP salvage
F	0004849	molecular_function	uridine kinase activity
F	0005524	molecular_function	ATP binding
F	0005575	cellular_component	cellular_component
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0009224	biological_process	CMP biosynthetic process
F	0016301	molecular_function	kinase activity
F	0042802	molecular_function	identical protein binding
F	0043771	molecular_function	cytidine kinase activity
F	0044206	biological_process	UMP salvage
F	0044211	biological_process	CTP salvage
G	0004849	molecular_function	uridine kinase activity
G	0005524	molecular_function	ATP binding
G	0005575	cellular_component	cellular_component
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0009224	biological_process	CMP biosynthetic process
G	0016301	molecular_function	kinase activity
G	0042802	molecular_function	identical protein binding
G	0043771	molecular_function	cytidine kinase activity
G	0044206	biological_process	UMP salvage
G	0044211	biological_process	CTP salvage
H	0004849	molecular_function	uridine kinase activity
H	0005524	molecular_function	ATP binding
H	0005575	cellular_component	cellular_component
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0009224	biological_process	CMP biosynthetic process
H	0016301	molecular_function	kinase activity
H	0042802	molecular_function	identical protein binding
H	0043771	molecular_function	cytidine kinase activity
H	0044206	biological_process	UMP salvage
H	0044211	biological_process	CTP salvage

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue PO4 A 301

Chain	Residue
A	THR29
A	ALA30
A	SER31
A	GLY32
A	LYS33
A	SER34
A	ARG169

site_id	AC2
Number of Residues	3
Details	binding site for residue GOL A 302

Chain	Residue
A	TYR203
A	PRO199
A	LYS202

site_id	AC3
Number of Residues	1
Details	binding site for residue GOL A 303

Chain	Residue
A	SER164

site_id	AC4
Number of Residues	5
Details	binding site for residue GOL A 304

Chain	Residue
A	GLN61
A	ASN91
A	LEU138
A	SER142
A	VAL145

site_id	AC5
Number of Residues	3
Details	binding site for residue GOL A 305

Chain	Residue
A	PHE81
A	HIS85
A	ASP87

site_id	AC6
Number of Residues	7
Details	binding site for residue PO4 B 301

Chain	Residue
B	THR29
B	ALA30
B	SER31
B	GLY32
B	LYS33
B	SER34
B	ARG169

site_id	AC7
Number of Residues	3
Details	binding site for residue GOL B 302

Chain	Residue
B	PHE81
B	ASN82
B	ASP87

site_id	AC8
Number of Residues	5
Details	binding site for residue GOL B 303

Chain	Residue
B	PRO199
B	LYS202
B	TYR203
B	HOH405
E	GLU195

site_id	AC9
Number of Residues	4
Details	binding site for residue GOL B 304

Chain	Residue
B	TYR65
B	TYR112
B	SER116
B	SER118

site_id	AD1
Number of Residues	8
Details	binding site for residue PO4 C 301

Chain	Residue
C	GLY28
C	THR29
C	ALA30
C	SER31
C	GLY32
C	LYS33
C	SER34
C	ARG169

site_id	AD2
Number of Residues	4
Details	binding site for residue GOL C 302

Chain	Residue
A	LEU182
A	ILE186
C	SER164
C	LEU168

site_id	AD3
Number of Residues	3
Details	binding site for residue GOL C 303

Chain	Residue
C	PRO128
C	ASP130
C	HOH402

site_id	AD4
Number of Residues	7
Details	binding site for residue GOL C 304

Chain	Residue
C	GLN61
C	PRO86
C	ASN91
C	ILE94
C	LEU138
C	ALA139
C	SER142

site_id	AD5
Number of Residues	1
Details	binding site for residue GOL C 305

Chain	Residue
C	LYS202

site_id	AD6
Number of Residues	7
Details	binding site for residue PO4 D 301

Chain	Residue
D	THR29
D	ALA30
D	SER31
D	GLY32
D	LYS33
D	SER34
D	ARG169

site_id	AD7
Number of Residues	4
Details	binding site for residue GOL D 302

Chain	Residue
B	GLU194
D	ASP158
D	ALA159
D	ASP160

site_id	AD8
Number of Residues	5
Details	binding site for residue GOL D 303

Chain	Residue
D	GLN61
D	PRO86
D	ASN91
D	LEU138
D	SER142

site_id	AD9
Number of Residues	2
Details	binding site for residue GOL D 304

Chain	Residue
D	PRO128
D	ASP130

site_id	AE1
Number of Residues	2
Details	binding site for residue GOL D 305

Chain	Residue
D	ASP227
E	GLY231

site_id	AE2
Number of Residues	1
Details	binding site for residue GOL D 306

Chain	Residue
D	ARG169

site_id	AE3
Number of Residues	4
Details	binding site for residue GOL D 307

Chain	Residue
D	LYS96
D	GLU100
D	VAL107
D	GLN108

site_id	AE4
Number of Residues	9
Details	binding site for residue UZ0 D 308

Chain	Residue
D	THR29
D	TYR65
D	PHE81
D	PHE83
D	ASP84
D	ARG166
D	GLN184
D	PHE188
D	VAL189

site_id	AE5
Number of Residues	5
Details	binding site for residue PO4 E 301

Chain	Residue
E	SER34
E	ALA30
E	SER31
E	GLY32
E	LYS33

site_id	AE6
Number of Residues	3
Details	binding site for residue GOL E 302

Chain	Residue
D	ILE207
E	ASP156
E	ASP158

site_id	AE7
Number of Residues	2
Details	binding site for residue GOL E 303

Chain	Residue
E	SER183
G	SER164

site_id	AE8
Number of Residues	4
Details	binding site for residue GOL E 304

Chain	Residue
E	TYR141
E	PRO199
E	LYS202
E	TYR203

site_id	AE9
Number of Residues	5
Details	binding site for residue GOL E 305

Chain	Residue
E	GLN61
E	PRO86
E	ASN91
E	LEU138
E	SER142

site_id	AF1
Number of Residues	7
Details	binding site for residue PO4 F 301

Chain	Residue
F	GLY28
F	THR29
F	ALA30
F	SER31
F	GLY32
F	LYS33
F	SER34

site_id	AF2
Number of Residues	2
Details	binding site for residue GOL F 302

Chain	Residue
F	GLU100
F	GLU103

site_id	AF3
Number of Residues	4
Details	binding site for residue GOL F 303

Chain	Residue
F	GLU179
F	SER183
F	ILE186
H	SER164

site_id	AF4
Number of Residues	7
Details	binding site for residue GOL F 304

Chain	Residue
F	GLN61
F	PRO86
F	PHE89
F	ASN91
F	ILE94
F	LEU138
F	SER142

site_id	AF5
Number of Residues	4
Details	binding site for residue GOL F 305

Chain	Residue
F	LEU93
F	GLU100
F	VAL107
F	GLN108

site_id	AF6
Number of Residues	3
Details	binding site for residue GOL F 306

Chain	Residue
F	LYS99
F	GLU103
F	LEU148

site_id	AF7
Number of Residues	7
Details	binding site for residue UZ0 F 307

Chain	Residue
E	SER172
E	GLU173
F	TYR65
F	ASP84
F	PHE114
F	ARG174
F	HOH401

site_id	AF8
Number of Residues	6
Details	binding site for residue PO4 G 301

Chain	Residue
G	ALA30
G	SER31
G	GLY32
G	LYS33
G	SER34
G	ARG169

site_id	AF9
Number of Residues	3
Details	binding site for residue GOL G 302

Chain	Residue
E	SER164
G	SER183
G	ILE186

site_id	AG1
Number of Residues	8
Details	binding site for residue PO4 H 301

Chain	Residue
H	GLY28
H	THR29
H	ALA30
H	SER31
H	GLY32
H	LYS33
H	SER34
H	ARG169

site_id	AG2
Number of Residues	11
Details	binding site for Di-peptide UZR E 306 and ARG E 174

Chain	Residue
E	PHE83
E	ARG169
E	ASP170
E	SER172
E	GLU173
E	GLY175
E	ARG176
F	GLU173
F	ARG174
F	GLY175
F	ARG176

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	64
Details	BINDING: BINDING => ECO:0000269\|PubMed:15130468, ECO:0000269\|PubMed:15735337

Chain	Residue	Details
A	GLY27
B	ASP84
B	TYR112
B	HIS117
B	ARG166
B	ARG176
B	GLN184
B	ASP213
C	GLY27
C	ASP84
C	TYR112
A	ASP84
C	HIS117
C	ARG166
C	ARG176
C	GLN184
C	ASP213
D	GLY27
D	ASP84
D	TYR112
D	HIS117
D	ARG166
A	TYR112
D	ARG176
D	GLN184
D	ASP213
E	GLY27
E	ASP84
E	TYR112
E	HIS117
E	ARG166
E	ARG176
E	GLN184
A	HIS117
E	ASP213
F	GLY27
F	ASP84
F	TYR112
F	HIS117
F	ARG166
F	ARG176
F	GLN184
F	ASP213
G	GLY27
A	ARG166
G	ASP84
G	TYR112
G	HIS117
G	ARG166
G	ARG176
G	GLN184
G	ASP213
H	GLY27
H	ASP84
H	TYR112
A	ARG176
H	HIS117
H	ARG166
H	ARG176
H	GLN184
H	ASP213
A	GLN184
A	ASP213
B	GLY27

site_id	SWS_FT_FI2
Number of Residues	8
Details	MOD_RES: N-acetylalanine => ECO:0007744\|PubMed:19413330

Chain	Residue	Details
A	ALA2
B	ALA2
C	ALA2
D	ALA2
E	ALA2
F	ALA2
G	ALA2
H	ALA2

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