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7DE3

Human adenylate kinase 1 (hAK1) mutant-R128W

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001520cellular_componentouter dense fiber
A0004017molecular_functionAMP kinase activity
A0004550molecular_functionnucleoside diphosphate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0006172biological_processADP biosynthetic process
A0009142biological_processnucleoside triphosphate biosynthetic process
A0015949biological_processnucleobase-containing small molecule interconversion
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0019205molecular_functionnucleobase-containing compound kinase activity
A0036126cellular_componentsperm flagellum
A0046033biological_processAMP metabolic process
A0046034biological_processATP metabolic process
A0046940biological_processnucleoside monophosphate phosphorylation
A0047506molecular_functiondAMP kinase activity
A0050145molecular_functionnucleoside monophosphate kinase activity
A0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00113
Number of Residues12
DetailsADENYLATE_KINASE Adenylate kinase signature. FLIDGYPRevqQ
ChainResidueDetails
APHE90-GLN101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues29
DetailsRegion: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_03171","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of human AK1A in complex with AP5A.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2005","submissionDatabase":"PDB data bank","title":"Structure of adenylate kinase 1 in complex with P1, P4-di(adenosine)tetraphosphate.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03171","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of human AK1A in complex with AP5A.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2005","submissionDatabase":"PDB data bank","title":"Structure of adenylate kinase 1 in complex with P1, P4-di(adenosine)tetraphosphate.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"HAMAP-Rule","id":"MF_03171","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"183954","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239803

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