3CM0
Crystal structure of adenylate kinase from Thermus thermophilus HB8
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004017 | molecular_function | AMP kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
A | 0009165 | biological_process | nucleotide biosynthetic process |
A | 0016301 | molecular_function | kinase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
A | 0044209 | biological_process | AMP salvage |
A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
Functional Information from PROSITE/UniProt
site_id | PS00113 |
Number of Residues | 12 |
Details | ADENYLATE_KINASE Adenylate kinase signature. VIFDGFPRtlaQ |
Chain | Residue | Details |
A | VAL80-GLN91 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 29 |
Details | Region: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2008","submissionDatabase":"PDB data bank","title":"Crystal structure of adenylate kinase from Thermus thermophilus HB8.","authors":["Nakagawa N.","Kondo N.","Masui R.","Yokoyama S.","Kuramitsu S."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | Region: {"description":"LID","evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2008","submissionDatabase":"PDB data bank","title":"Crystal structure of adenylate kinase from Thermus thermophilus HB8.","authors":["Nakagawa N.","Kondo N.","Masui R.","Yokoyama S.","Kuramitsu S."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 17 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1zio |
Chain | Residue | Details |
A | ASP135 | |
A | LYS17 | |
A | ARG126 | |
A | ARG143 | |
A | ASP134 | |
A | ARG132 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1zio |
Chain | Residue | Details |
A | LYS17 | |
A | ASP37 | |
A | ARG125 | |
A | ASP168 |