1UKY
SUBSTRATE SPECIFICITY AND ASSEMBLY OF CATALYTIC CENTER DERIVED FROM TWO STRUCTURES OF LIGATED URIDYLATE KINASE
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 | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| A | 0006225 | biological_process | UDP biosynthetic process |
| A | 0009123 | biological_process | nucleoside monophosphate metabolic process |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
| A | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| A | 0033862 | molecular_function | UMP kinase activity |
| A | 0046705 | biological_process | CDP biosynthetic process |
| A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
| A | 0072528 | biological_process | pyrimidine-containing compound biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ADP A 205 |
| Chain | Residue |
| A | GLY26 |
| A | SER188 |
| A | VAL189 |
| A | ADP206 |
| A | HOH308 |
| A | HOH309 |
| A | HOH326 |
| A | HOH339 |
| A | HOH351 |
| A | HOH361 |
| A | HOH377 |
| A | ALA27 |
| A | GLY28 |
| A | LYS29 |
| A | GLY30 |
| A | THR31 |
| A | ARG138 |
| A | ARG142 |
| A | ARG187 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ADP A 206 |
| Chain | Residue |
| A | PRO25 |
| A | LYS29 |
| A | LEU51 |
| A | ARG52 |
| A | ILE70 |
| A | GLN74 |
| A | ILE75 |
| A | VAL76 |
| A | GLY104 |
| A | PHE105 |
| A | ARG107 |
| A | GLN111 |
| A | ARG142 |
| A | ARG148 |
| A | ARG159 |
| A | ADP205 |
| A | HOH303 |
| A | HOH313 |
| A | HOH359 |
| A | HOH375 |
| A | HOH389 |
Functional Information from PROSITE/UniProt
| site_id | PS00113 |
| Number of Residues | 12 |
| Details | ADENYLATE_KINASE Adenylate kinase signature. FLIDGFPRkmdQ |
| Chain | Residue | Details |
| A | PHE100-GLN111 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 30 |
| Details | Region: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_03172","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7877173","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8107116","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Region: {"description":"LID","evidences":[{"source":"HAMAP-Rule","id":"MF_03172","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7877173","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8107116","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03172","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7877173","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8107116","evidenceCode":"ECO:0000269"}]} |
| 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 | ARG142 | |
| A | ARG148 | |
| A | ASP151 | |
| A | ASP150 | |
| A | ARG159 | |
| A | LYS29 |
