Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2I6A

Human Adenosine Kinase in Complex With 5'-Deoxy-5-Iodotubercidin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003723	molecular_function	RNA binding
A	0004001	molecular_function	adenosine kinase activity
A	0004136	molecular_function	deoxyadenosine kinase activity
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006144	biological_process	purine nucleobase metabolic process
A	0006166	biological_process	purine ribonucleoside salvage
A	0006170	biological_process	dAMP biosynthetic process
A	0009156	biological_process	ribonucleoside monophosphate biosynthetic process
A	0016301	molecular_function	kinase activity
A	0032261	biological_process	purine nucleotide salvage
A	0032263	biological_process	GMP salvage
A	0044209	biological_process	AMP salvage
A	0110052	biological_process	toxic metabolite repair
B	0003723	molecular_function	RNA binding
B	0004001	molecular_function	adenosine kinase activity
B	0004136	molecular_function	deoxyadenosine kinase activity
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006144	biological_process	purine nucleobase metabolic process
B	0006166	biological_process	purine ribonucleoside salvage
B	0006170	biological_process	dAMP biosynthetic process
B	0009156	biological_process	ribonucleoside monophosphate biosynthetic process
B	0016301	molecular_function	kinase activity
B	0032261	biological_process	purine nucleotide salvage
B	0032263	biological_process	GMP salvage
B	0044209	biological_process	AMP salvage
B	0110052	biological_process	toxic metabolite repair
C	0003723	molecular_function	RNA binding
C	0004001	molecular_function	adenosine kinase activity
C	0004136	molecular_function	deoxyadenosine kinase activity
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006144	biological_process	purine nucleobase metabolic process
C	0006166	biological_process	purine ribonucleoside salvage
C	0006170	biological_process	dAMP biosynthetic process
C	0009156	biological_process	ribonucleoside monophosphate biosynthetic process
C	0016301	molecular_function	kinase activity
C	0032261	biological_process	purine nucleotide salvage
C	0032263	biological_process	GMP salvage
C	0044209	biological_process	AMP salvage
C	0110052	biological_process	toxic metabolite repair
D	0003723	molecular_function	RNA binding
D	0004001	molecular_function	adenosine kinase activity
D	0004136	molecular_function	deoxyadenosine kinase activity
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006144	biological_process	purine nucleobase metabolic process
D	0006166	biological_process	purine ribonucleoside salvage
D	0006170	biological_process	dAMP biosynthetic process
D	0009156	biological_process	ribonucleoside monophosphate biosynthetic process
D	0016301	molecular_function	kinase activity
D	0032261	biological_process	purine nucleotide salvage
D	0032263	biological_process	GMP salvage
D	0044209	biological_process	AMP salvage
D	0110052	biological_process	toxic metabolite repair

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 5I5 A 500

Chain	Residue
A	ASN14
A	PHE170
A	ASN296
A	ASP300
A	ASP18
A	ILE39
A	LEU40
A	GLY63
A	GLY64
A	SER65
A	ASN68
A	CYS123

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 5I5 B 500

Chain	Residue
B	ASN14
B	ASP18
B	ILE39
B	LEU40
B	GLY63
B	GLY64
B	SER65
B	ASN68
B	ALA136
B	PHE170
B	ASN296
B	ASP300

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 5I5 C 500

Chain	Residue
C	ASN14
C	ASP18
C	ILE39
C	LEU40
C	GLY63
C	GLY64
C	SER65
C	ASN68
C	ALA136
C	LEU138
C	PHE170
C	ASN296
C	ASP300

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 5I5 D 500

Chain	Residue
D	ASN14
D	ASP18
D	ILE39
D	LEU40
D	GLY64
D	SER65
D	ASN68
D	CYS123
D	ALA136
D	PHE170
D	ASN296
D	ASP300
D	HOH555

Functional Information from PROSITE/UniProt

site_id	PS00584
Number of Residues	14
Details	PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTnGAGDafvGGFL

Chain	Residue	Details
A	ASP294-LEU307

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"9843365","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BX4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9843365","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BX4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"12112843","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1lio

Chain	Residue	Details
A	ASP300
A	ARG132

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1lio

Chain	Residue	Details
B	ASP300
B	ARG132

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1lio

Chain	Residue	Details
C	ASP300
C	ARG132

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1lio

Chain	Residue	Details
D	ASP300
D	ARG132

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1lio

Chain	Residue	Details
A	ALA298
A	ASP300
A	GLY297
A	GLY299

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1lio

Chain	Residue	Details
B	ALA298
B	ASP300
B	GLY297
B	GLY299

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1lio

Chain	Residue	Details
C	ALA298
C	ASP300
C	GLY297
C	GLY299

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1lio

Chain	Residue	Details
D	ALA298
D	ASP300
D	GLY297
D	GLY299

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)