5EJE
Crystal structure of E. coli Adenylate kinase G56C/T163C double mutant in complex with Ap5a
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004017 | molecular_function | adenylate kinase activity |
| A | 0004550 | molecular_function | nucleoside diphosphate kinase activity |
| A | 0005515 | molecular_function | protein binding |
| 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 | 0006172 | biological_process | ADP biosynthetic 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 | 0015951 | biological_process | purine ribonucleotide interconversion |
| A | 0016208 | molecular_function | AMP binding |
| 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 | 0000287 | molecular_function | magnesium ion binding |
| B | 0004017 | molecular_function | adenylate kinase activity |
| B | 0004550 | molecular_function | nucleoside diphosphate kinase activity |
| B | 0005515 | molecular_function | protein binding |
| 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 | 0006172 | biological_process | ADP biosynthetic 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 | 0015951 | biological_process | purine ribonucleotide interconversion |
| B | 0016208 | molecular_function | AMP binding |
| 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 | 39 |
| Details | binding site for residue AP5 A 301 |
| Chain | Residue |
| A | PRO9 |
| A | LEU35 |
| A | ARG36 |
| A | MET53 |
| A | LYS57 |
| A | VAL59 |
| A | VAL64 |
| A | GLY85 |
| A | PHE86 |
| A | ARG88 |
| A | GLN92 |
| A | GLY10 |
| A | ARG119 |
| A | ARG123 |
| A | VAL132 |
| A | TYR133 |
| A | HIS134 |
| A | PHE137 |
| A | ARG156 |
| A | ARG167 |
| A | LYS200 |
| A | VAL202 |
| A | ALA11 |
| A | CO302 |
| A | HOH425 |
| A | HOH428 |
| A | HOH441 |
| A | HOH454 |
| A | HOH458 |
| A | HOH459 |
| A | HOH474 |
| A | HOH496 |
| A | HOH515 |
| A | GLY12 |
| A | LYS13 |
| A | GLY14 |
| A | THR15 |
| A | THR31 |
| A | GLY32 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CO A 302 |
| Chain | Residue |
| A | AP5301 |
| A | HOH402 |
| A | HOH428 |
| A | HOH454 |
| A | HOH458 |
| site_id | AC3 |
| Number of Residues | 40 |
| Details | binding site for residue AP5 B 301 |
| Chain | Residue |
| B | PRO9 |
| B | GLY10 |
| B | ALA11 |
| B | GLY12 |
| B | LYS13 |
| B | GLY14 |
| B | THR15 |
| B | THR31 |
| B | GLY32 |
| B | LEU35 |
| B | ARG36 |
| B | MET53 |
| B | LYS57 |
| B | LEU58 |
| B | VAL59 |
| B | VAL64 |
| B | GLY85 |
| B | PHE86 |
| B | ARG88 |
| B | GLN92 |
| B | ARG119 |
| B | ARG123 |
| B | TYR133 |
| B | HIS134 |
| B | PHE137 |
| B | ARG156 |
| B | ARG167 |
| B | LYS200 |
| B | VAL202 |
| B | CO302 |
| B | HOH402 |
| B | HOH434 |
| B | HOH441 |
| B | HOH442 |
| B | HOH445 |
| B | HOH462 |
| B | HOH466 |
| B | HOH468 |
| B | HOH473 |
| B | HOH494 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue CO B 302 |
| Chain | Residue |
| B | AP5301 |
| B | HOH402 |
| B | HOH442 |
| B | HOH462 |
| B | HOH466 |
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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:16302237, ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:7937733, ECO:0000269|PubMed:8451239 |
| Chain | Residue | Details |
| A | GLY10 | |
| B | THR31 | |
| B | ARG36 | |
| B | LYS57 | |
| B | GLN92 | |
| B | ARG123 | |
| B | ARG156 | |
| B | LYS200 | |
| A | THR31 | |
| A | ARG36 | |
| A | LYS57 | |
| A | GLN92 | |
| A | ARG123 | |
| A | ARG156 | |
| A | LYS200 | |
| B | GLY10 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:8451239 |
| Chain | Residue | Details |
| A | GLY85 | |
| A | ARG167 | |
| B | GLY85 | |
| B | ARG167 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:16302237, ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:8451239 |
| Chain | Residue | Details |
| A | VAL132 | |
| B | VAL132 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS192 | |
| B | LYS192 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16302237 |
| Chain | Residue | Details |
| A | ARG119 | |
| B | ARG119 |
