3GMT
Crystal structure of adenylate kinase from burkholderia pseudomallei
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004017 | molecular_function | adenylate 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 | 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 | 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 | 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 | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 301 |
| Chain | Residue |
| A | GLY10 |
| A | ALA11 |
| A | GLY12 |
| A | LYS13 |
| A | GLY14 |
| A | HOH322 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| A | ARG119 |
| A | MSE120 |
| A | ARG123 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 301 |
| Chain | Residue |
| B | GLY10 |
| B | ALA11 |
| B | GLY12 |
| B | LYS13 |
| B | GLY14 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 302 |
| Chain | Residue |
| B | ARG119 |
| B | MSE120 |
| B | ARG123 |
Functional Information from PROSITE/UniProt
| site_id | PS00113 |
| Number of Residues | 12 |
| Details | ADENYLATE_KINASE Adenylate kinase signature. YLFDGFPRtiaQ |
| Chain | Residue | Details |
| A | TYR81-GLN92 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235 |
| Chain | Residue | Details |
| A | GLY10 | |
| A | ARG167 | |
| A | GLY206 | |
| B | GLY10 | |
| B | THR31 | |
| B | ARG36 | |
| B | LYS57 | |
| B | GLY85 | |
| B | GLN92 | |
| B | ARG123 | |
| B | THR132 | |
| A | THR31 | |
| B | ARG156 | |
| B | ARG167 | |
| B | GLY206 | |
| A | ARG36 | |
| A | LYS57 | |
| A | GLY85 | |
| A | GLN92 | |
| A | ARG123 | |
| A | THR132 | |
| A | ARG156 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1zio |
| Chain | Residue | Details |
| A | LYS13 | |
| A | ARG156 | |
| A | ARG123 | |
| A | ARG167 | |
| A | ASP158 | |
| A | ASP159 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1zio |
| Chain | Residue | Details |
| B | LYS13 | |
| B | ARG156 | |
| B | ARG123 | |
| B | ARG167 | |
| B | ASP158 | |
| B | ASP159 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1zio |
| Chain | Residue | Details |
| A | LYS13 | |
| A | ARG123 | |
| A | ASP33 | |
| A | ASP159 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1zio |
| Chain | Residue | Details |
| B | LYS13 | |
| B | ARG123 | |
| B | ASP33 | |
| B | ASP159 |
