7DE3
Human adenylate kinase 1 (hAK1) mutant-R128W
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0001520 | cellular_component | outer dense fiber |
A | 0004017 | molecular_function | AMP kinase activity |
A | 0004550 | molecular_function | nucleoside diphosphate kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
A | 0006172 | biological_process | ADP biosynthetic process |
A | 0009142 | biological_process | nucleoside triphosphate biosynthetic process |
A | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
A | 0016301 | molecular_function | kinase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
A | 0036126 | cellular_component | sperm flagellum |
A | 0046033 | biological_process | AMP metabolic process |
A | 0046034 | biological_process | ATP metabolic process |
A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
A | 0047506 | molecular_function | dAMP kinase activity |
A | 0050145 | molecular_function | nucleoside monophosphate kinase activity |
A | 0070062 | cellular_component | extracellular exosome |
Functional Information from PROSITE/UniProt
site_id | PS00113 |
Number of Residues | 12 |
Details | ADENYLATE_KINASE Adenylate kinase signature. FLIDGYPRevqQ |
Chain | Residue | Details |
A | PHE90-GLN101 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 29 |
Details | Region: {"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)"]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | Binding 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)"]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"HAMAP-Rule","id":"MF_03171","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"183954","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |