4JLD
Crystal Structures of adenylate kinase with 2 ADP's
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004017 | molecular_function | AMP 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 | 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 | 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 | 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 | 21 |
| Details | BINDING SITE FOR RESIDUE ADP A 301 |
| Chain | Residue |
| A | GLY10 |
| A | TYR134 |
| A | HIS135 |
| A | TYR138 |
| A | LYS189 |
| A | PRO190 |
| A | VAL191 |
| A | ADP302 |
| A | HOH403 |
| A | HOH420 |
| A | HOH446 |
| A | ALA11 |
| A | HOH542 |
| B | ARG55 |
| A | GLY12 |
| A | LYS13 |
| A | GLY14 |
| A | THR15 |
| A | ARG120 |
| A | ARG124 |
| A | VAL133 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ADP A 302 |
| Chain | Residue |
| A | PRO9 |
| A | THR31 |
| A | GLY32 |
| A | LEU35 |
| A | ARG36 |
| A | MET53 |
| A | GLU57 |
| A | VAL59 |
| A | ILE64 |
| A | GLY82 |
| A | ARG85 |
| A | GLN89 |
| A | ARG124 |
| A | ARG150 |
| A | ARG161 |
| A | ADP301 |
| A | HOH402 |
| A | HOH412 |
| A | HOH429 |
| A | HOH431 |
| A | HOH437 |
| A | HOH451 |
| A | HOH616 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ADP B 301 |
| Chain | Residue |
| B | GLY10 |
| B | ALA11 |
| B | GLY12 |
| B | LYS13 |
| B | GLY14 |
| B | THR15 |
| B | ARG120 |
| B | ARG124 |
| B | TYR134 |
| B | HIS135 |
| B | TYR138 |
| B | LYS189 |
| B | PRO190 |
| B | VAL191 |
| B | ADP302 |
| B | HOH404 |
| B | HOH418 |
| B | HOH424 |
| B | HOH477 |
| B | HOH535 |
| B | HOH644 |
| B | HOH647 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ADP B 302 |
| Chain | Residue |
| B | THR31 |
| B | GLY32 |
| B | LEU35 |
| B | ARG36 |
| B | MET53 |
| B | GLU57 |
| B | LEU58 |
| B | VAL59 |
| B | ILE64 |
| B | GLY82 |
| B | ARG85 |
| B | GLN89 |
| B | ARG150 |
| B | ARG161 |
| B | ADP301 |
| B | HOH401 |
| B | HOH415 |
| B | HOH423 |
| B | HOH451 |
| B | HOH644 |
| B | HOH647 |
Functional Information from PROSITE/UniProt
| site_id | PS00113 |
| Number of Residues | 12 |
| Details | ADENYLATE_KINASE Adenylate kinase signature. VIFDGFPRtvkQ |
| Chain | Residue | Details |
| A | VAL78-GLN89 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 58 |
| Details | Region: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18026086","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 60 |
| Details | Region: {"description":"LID","evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18026086","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 34 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18026086","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
