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2I6B

Human Adenosine Kinase in Complex with An Acetylinic Inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003723molecular_functionRNA binding
A0004001molecular_functionadenosine kinase activity
A0004136molecular_functiondeoxyadenosine kinase activity
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006144biological_processpurine nucleobase metabolic process
A0006166biological_processpurine ribonucleoside salvage
A0006175biological_processdATP biosynthetic process
A0009156biological_processribonucleoside monophosphate biosynthetic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0032263biological_processGMP salvage
A0044209biological_processAMP salvage
A0046872molecular_functionmetal ion binding
A0106383biological_processdAMP salvage
B0000166molecular_functionnucleotide binding
B0003723molecular_functionRNA binding
B0004001molecular_functionadenosine kinase activity
B0004136molecular_functiondeoxyadenosine kinase activity
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006144biological_processpurine nucleobase metabolic process
B0006166biological_processpurine ribonucleoside salvage
B0006175biological_processdATP biosynthetic process
B0009156biological_processribonucleoside monophosphate biosynthetic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0032263biological_processGMP salvage
B0044209biological_processAMP salvage
B0046872molecular_functionmetal ion binding
B0106383biological_processdAMP salvage
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 89I A 500
ChainResidue
AASN14
APHE201
ATYR206
BPHE205
B89I500
AGLN38
AILE39
AGLY64
ASER65
AALA136
ALEU138
APHE170
ATHR173

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 89I B 500
ChainResidue
APHE205
A89I500
BGLN38
BILE39
BLEU40
BSER65
BLEU138
BPHE170
BTYR206
BHOH585

Functional Information from PROSITE/UniProt
site_idPS00584
Number of Residues14
DetailsPFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTnGAGDafvGGFL
ChainResidueDetails
AASP294-LEU307

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"9843365","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BX4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9843365","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BX4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"12112843","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1lio
ChainResidueDetails
AASP300
AARG132

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1lio
ChainResidueDetails
BASP300
BARG132

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1lio
ChainResidueDetails
AALA298
AASP300
AGLY297
AGLY299

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1lio
ChainResidueDetails
BALA298
BASP300
BGLY297
BGLY299

239803

PDB entries from 2025-08-06

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