1UKZ
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 | adenylate kinase activity |
| A | 0004127 | molecular_function | cytidylate kinase activity |
| A | 0004550 | molecular_function | nucleoside diphosphate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0009041 | molecular_function | UMP/dUMP kinase activity |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0016740 | molecular_function | transferase activity |
| 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 | 21 |
| Details | BINDING SITE FOR RESIDUE ADP A 205 |
| Chain | Residue |
| A | GLY26 |
| A | ARG187 |
| A | SER188 |
| A | VAL189 |
| A | HOH308 |
| A | HOH309 |
| A | HOH316 |
| A | HOH317 |
| A | HOH345 |
| A | HOH347 |
| A | HOH349 |
| A | ALA27 |
| A | HOH363 |
| A | HOH393 |
| A | GLY28 |
| A | LYS29 |
| A | GLY30 |
| A | THR31 |
| A | ALA58 |
| A | ARG138 |
| A | ARG142 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE AMP A 206 |
| Chain | Residue |
| A | ALA47 |
| A | LEU51 |
| A | ARG52 |
| A | CYS69 |
| A | ILE70 |
| A | GLN74 |
| A | ILE75 |
| A | VAL76 |
| A | THR81 |
| A | GLY104 |
| A | PHE105 |
| A | ARG107 |
| A | GLN111 |
| A | ARG148 |
| A | ARG159 |
| A | HOH302 |
| A | HOH305 |
| A | HOH310 |
| A | HOH316 |
| A | HOH317 |
| A | HOH329 |
| A | HOH356 |
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 | 9 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:7877173, ECO:0000269|PubMed:8107116 |
| Chain | Residue | Details |
| A | GLY26 | |
| A | ARG52 | |
| A | GLN74 | |
| A | GLY104 | |
| A | GLN111 | |
| A | ARG142 | |
| A | ARG148 | |
| A | ARG159 | |
| A | ARG187 |
