Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2OCP

Crystal Structure of Human Deoxyguanosine Kinase

Replaces: 1JAG

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0019136	molecular_function	deoxynucleoside kinase activity
B	0005524	molecular_function	ATP binding
B	0006139	biological_process	nucleobase-containing compound metabolic process
B	0019136	molecular_function	deoxynucleoside kinase activity
C	0005524	molecular_function	ATP binding
C	0006139	biological_process	nucleobase-containing compound metabolic process
C	0019136	molecular_function	deoxynucleoside kinase activity
D	0005524	molecular_function	ATP binding
D	0006139	biological_process	nucleobase-containing compound metabolic process
D	0019136	molecular_function	deoxynucleoside kinase activity
E	0005524	molecular_function	ATP binding
E	0006139	biological_process	nucleobase-containing compound metabolic process
E	0019136	molecular_function	deoxynucleoside kinase activity
F	0005524	molecular_function	ATP binding
F	0006139	biological_process	nucleobase-containing compound metabolic process
F	0019136	molecular_function	deoxynucleoside kinase activity
G	0005524	molecular_function	ATP binding
G	0006139	biological_process	nucleobase-containing compound metabolic process
G	0019136	molecular_function	deoxynucleoside kinase activity
H	0005524	molecular_function	ATP binding
H	0006139	biological_process	nucleobase-containing compound metabolic process
H	0019136	molecular_function	deoxynucleoside kinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE DTP A 301

Chain	Residue
A	ILE47
A	ARG118
A	ARG142
A	ASP147
A	PHE151
A	ARG206
A	ARG208
A	GLU211
A	HOH321
A	ALA48
A	LYS51
A	SER52
A	VAL72
A	LEU96
A	TYR100
A	PHE110
A	GLN111

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE DTP B 301

Chain	Residue
B	ILE47
B	ALA48
B	LYS51
B	SER52
B	VAL72
B	LEU96
B	TYR100
B	PHE110
B	GLN111
B	ARG118
B	ARG142
B	PHE151
B	ARG206
B	ARG208
B	GLU211
B	HOH323

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE DTP C 301

Chain	Residue
C	ILE47
C	ALA48
C	LYS51
C	SER52
C	VAL72
C	LEU96
C	TYR100
C	PHE110
C	GLN111
C	ARG118
C	ARG142
C	PHE151
C	ARG206
C	ARG208
C	GLU211
C	HOH322

site_id	AC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE DTP D 301

Chain	Residue
D	ILE47
D	ALA48
D	LYS51
D	SER52
D	VAL72
D	LEU96
D	TYR100
D	PHE110
D	GLN111
D	ARG118
D	ARG142
D	ASP147
D	PHE151
D	ARG206
D	ARG208
D	GLU211
D	HOH323

site_id	AC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE DTP E 301

Chain	Residue
E	ILE47
E	ALA48
E	LYS51
E	SER52
E	VAL72
E	LEU96
E	TYR100
E	PHE110
E	GLN111
E	ARG118
E	ARG142
E	PHE151
E	ARG206
E	ARG208
E	GLU211
E	HOH522

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE DTP F 301

Chain	Residue
F	ILE47
F	ALA48
F	LYS51
F	SER52
F	VAL72
F	LEU96
F	TYR100
F	PHE110
F	GLN111
F	ARG118
F	ARG142
F	ASP147
F	PHE151
F	ARG206
F	ARG208
F	GLU211
F	HOH622

site_id	AC7
Number of Residues	16
Details	BINDING SITE FOR RESIDUE DTP G 301

Chain	Residue
G	ILE47
G	ALA48
G	LYS51
G	SER52
G	VAL72
G	LEU96
G	TYR100
G	PHE110
G	GLN111
G	ARG118
G	ARG142
G	PHE151
G	ARG206
G	ARG208
G	GLU211
G	HOH722

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE DTP H 301

Chain	Residue
H	ILE47
H	ALA48
H	LYS51
H	SER52
H	VAL72
H	LEU96
H	TYR100
H	PHE110
H	GLN111
H	ARG118
H	ARG142
H	PHE151
H	ARG206
H	ARG208
H	GLU211
H	HOH822

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	GLU141
B	GLU141
C	GLU141
D	GLU141
E	GLU141
F	GLU141
G	GLU141
H	GLU141

site_id	SWS_FT_FI2
Number of Residues	64
Details	BINDING: BINDING => ECO:0000269\|PubMed:11427893, ECO:0007744\|PDB:2OCP

Chain	Residue	Details
A	GLY45
B	GLU70
B	TYR100
B	GLN111
B	ARG118
B	ARG142
B	ARG206
B	GLU211
C	GLY45
C	GLU70
C	TYR100
A	GLU70
C	GLN111
C	ARG118
C	ARG142
C	ARG206
C	GLU211
D	GLY45
D	GLU70
D	TYR100
D	GLN111
D	ARG118
A	TYR100
D	ARG142
D	ARG206
D	GLU211
E	GLY45
E	GLU70
E	TYR100
E	GLN111
E	ARG118
E	ARG142
E	ARG206
A	GLN111
E	GLU211
F	GLY45
F	GLU70
F	TYR100
F	GLN111
F	ARG118
F	ARG142
F	ARG206
F	GLU211
G	GLY45
A	ARG118
G	GLU70
G	TYR100
G	GLN111
G	ARG118
G	ARG142
G	ARG206
G	GLU211
H	GLY45
H	GLU70
H	TYR100
A	ARG142
H	GLN111
H	ARG118
H	ARG142
H	ARG206
H	GLU211
A	ARG206
A	GLU211
B	GLY45

site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING: BINDING => ECO:0000255

Chain	Residue	Details
A	ASP147
E	ASP254
F	ASP147
F	ASP254
G	ASP147
G	ASP254
H	ASP147
H	ASP254
A	ASP254
B	ASP147
B	ASP254
C	ASP147
C	ASP254
D	ASP147
D	ASP254
E	ASP147

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS275
B	LYS275
C	LYS275
D	LYS275
E	LYS275
F	LYS275
G	LYS275
H	LYS275

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 15896737, 12363036, 14623087

Chain	Residue	Details
A	ARG142
A	GLU70

site_id	MCSA1
Number of Residues	2
Details	M-CSA 615

Chain	Residue	Details
A	GLU70	activator, proton acceptor, proton donor
A	ARG142	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	2
Details	M-CSA 615

Chain	Residue	Details
B	GLU70	activator, proton acceptor, proton donor
B	ARG142	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA3
Number of Residues	2
Details	M-CSA 615

Chain	Residue	Details
C	GLU70	activator, proton acceptor, proton donor
C	ARG142	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA4
Number of Residues	2
Details	M-CSA 615

Chain	Residue	Details
D	GLU70	activator, proton acceptor, proton donor
D	ARG142	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA5
Number of Residues	2
Details	M-CSA 615

Chain	Residue	Details
E	GLU70	activator, proton acceptor, proton donor
E	ARG142	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA6
Number of Residues	2
Details	M-CSA 615

Chain	Residue	Details
F	GLU70	activator, proton acceptor, proton donor
F	ARG142	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA7
Number of Residues	2
Details	M-CSA 615

Chain	Residue	Details
G	GLU70	activator, proton acceptor, proton donor
G	ARG142	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA8
Number of Residues	2
Details	M-CSA 615

Chain	Residue	Details
H	GLU70	activator, proton acceptor, proton donor
H	ARG142	electrostatic stabiliser, hydrogen bond donor

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