4QBG
Crystal structure of a stable adenylate kinase variant AKlse4
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0008270 | molecular_function | zinc ion binding |
| 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 | 0046872 | molecular_function | metal ion binding |
| B | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 301 |
| Chain | Residue |
| B | CYS130 |
| B | CYS133 |
| B | CYS150 |
| B | ASP153 |
| site_id | AC2 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE AP5 B 302 |
| Chain | Residue |
| B | GLY14 |
| B | THR15 |
| B | THR31 |
| B | GLY32 |
| B | ARG36 |
| B | ILE53 |
| B | GLU57 |
| B | VAL59 |
| B | THR64 |
| B | GLY85 |
| B | PHE86 |
| B | ARG88 |
| B | GLN92 |
| B | ARG123 |
| B | ARG127 |
| B | ARG171 |
| B | GLN199 |
| B | MET201 |
| B | MG303 |
| B | HOH407 |
| B | HOH412 |
| B | HOH424 |
| B | HOH428 |
| B | HOH441 |
| B | HOH446 |
| B | HOH451 |
| B | HOH452 |
| B | HOH456 |
| B | HOH478 |
| B | HOH512 |
| B | HOH513 |
| B | HOH529 |
| B | HOH560 |
| B | PRO9 |
| B | GLY10 |
| B | ALA11 |
| B | GLY12 |
| B | LYS13 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 303 |
| Chain | Residue |
| B | AP5302 |
| B | HOH424 |
| B | HOH428 |
| B | HOH438 |
| B | HOH456 |
Functional Information from PROSITE/UniProt
| site_id | PS00113 |
| Number of Residues | 12 |
| Details | ADENYLATE_KINASE Adenylate kinase signature. FLLDGFPRtvaQ |
| Chain | Residue | Details |
| B | PHE81-GLN92 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 29 |
| Details | Region: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15100224","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16713575","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 37 |
| Details | Region: {"description":"LID","evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15100224","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16713575","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15100224","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16713575","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
