3X2S
Crystal structure of pyrene-conjugated adenylate 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 | 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 | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
| A | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| A | 0044209 | biological_process | AMP salvage |
| A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004017 | molecular_function | AMP kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| B | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
| B | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| B | 0044209 | biological_process | AMP salvage |
| B | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE JPY A 301 |
| Chain | Residue |
| A | CYS55 |
| A | LYS166 |
| A | GLU170 |
| A | JPY302 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE JPY A 302 |
| Chain | Residue |
| B | LEU67 |
| B | GLU70 |
| B | ARG71 |
| B | GLN74 |
| B | PRO128 |
| A | CYS169 |
| A | GLU170 |
| A | GLN173 |
| A | JPY301 |
| B | MET34 |
| site_id | AC3 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE AP5 A 303 |
| Chain | Residue |
| A | PRO9 |
| A | GLY10 |
| A | ALA11 |
| A | GLY12 |
| A | LYS13 |
| A | GLY14 |
| A | THR15 |
| A | THR31 |
| A | GLY32 |
| A | ARG36 |
| A | MET53 |
| A | LYS57 |
| A | LEU58 |
| A | VAL59 |
| A | VAL64 |
| A | GLY85 |
| A | PHE86 |
| A | ARG88 |
| A | GLN92 |
| A | ARG119 |
| A | ARG123 |
| A | VAL132 |
| A | TYR133 |
| A | HIS134 |
| A | PHE137 |
| A | ARG156 |
| A | ARG167 |
| A | LYS200 |
| A | PRO201 |
| A | VAL202 |
| A | MG304 |
| A | HOH401 |
| A | HOH403 |
| A | HOH405 |
| A | HOH407 |
| A | HOH408 |
| A | HOH410 |
| B | GLU114 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 304 |
| Chain | Residue |
| A | GLY14 |
| A | AP5303 |
| A | HOH401 |
| A | HOH406 |
| A | HOH407 |
| A | HOH408 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE JPY B 301 |
| Chain | Residue |
| A | ALA37 |
| B | CYS55 |
| B | LYS57 |
| B | LYS166 |
| B | JPY302 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE JPY B 302 |
| Chain | Residue |
| A | MET34 |
| A | LEU67 |
| A | GLU70 |
| A | ARG71 |
| A | GLN74 |
| B | CYS169 |
| B | GLU170 |
| B | GLN173 |
| B | JPY301 |
| site_id | AC7 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE AP5 B 303 |
| Chain | Residue |
| B | ARG167 |
| B | GLY198 |
| B | LYS200 |
| B | PRO201 |
| B | VAL202 |
| B | MG304 |
| B | HOH401 |
| B | HOH406 |
| B | HOH407 |
| B | HOH408 |
| B | HOH409 |
| B | HOH410 |
| A | GLU114 |
| B | PRO9 |
| B | GLY10 |
| B | ALA11 |
| B | GLY12 |
| B | LYS13 |
| B | GLY14 |
| B | THR15 |
| B | THR31 |
| B | GLY32 |
| B | LEU35 |
| B | ARG36 |
| B | LYS57 |
| B | LEU58 |
| B | VAL59 |
| B | VAL64 |
| B | GLY85 |
| B | PHE86 |
| B | ARG88 |
| B | GLN92 |
| B | ARG119 |
| B | ARG123 |
| B | VAL132 |
| B | TYR133 |
| B | HIS134 |
| B | PHE137 |
| B | ARG156 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 304 |
| Chain | Residue |
| B | GLY14 |
| B | AP5303 |
| B | HOH401 |
| B | HOH402 |
| B | HOH406 |
| B | HOH407 |
Functional Information from PROSITE/UniProt
| site_id | PS00113 |
| Number of Residues | 12 |
| Details | ADENYLATE_KINASE Adenylate kinase signature. FLLDGFPRtipQ |
| Chain | Residue | Details |
| A | PHE81-GLN92 |
