3X2S
Crystal structure of pyrene-conjugated adenylate kinase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004017 | molecular_function | adenylate 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 | 0009123 | biological_process | nucleoside monophosphate metabolic process |
A | 0009132 | biological_process | nucleoside diphosphate metabolic process |
A | 0009165 | biological_process | nucleotide biosynthetic process |
A | 0016301 | molecular_function | kinase 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 |
A | 0050145 | molecular_function | nucleoside monophosphate kinase activity |
B | 0004017 | molecular_function | adenylate kinase activity |
B | 0004550 | molecular_function | nucleoside diphosphate kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
B | 0009123 | biological_process | nucleoside monophosphate metabolic process |
B | 0009132 | biological_process | nucleoside diphosphate metabolic process |
B | 0009165 | biological_process | nucleotide biosynthetic process |
B | 0016301 | molecular_function | kinase 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 |
B | 0050145 | molecular_function | nucleoside monophosphate kinase activity |
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 |