4MKH
Crystal structure of a stable adenylate kinase variant AKv18
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 | 0008270 | molecular_function | zinc ion binding |
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 | 0046872 | molecular_function | metal ion binding |
A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
A | 0050145 | molecular_function | nucleoside monophosphate kinase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 301 |
Chain | Residue |
A | CYS130 |
A | CYS133 |
A | CYS150 |
A | ASP153 |
site_id | AC2 |
Number of Residues | 37 |
Details | BINDING SITE FOR RESIDUE AP5 A 302 |
Chain | Residue |
A | GLY14 |
A | THR15 |
A | THR31 |
A | GLY32 |
A | ARG36 |
A | ILE53 |
A | GLU57 |
A | LEU58 |
A | VAL59 |
A | THR64 |
A | GLY85 |
A | PHE86 |
A | ARG88 |
A | GLN92 |
A | ARG123 |
A | LEU124 |
A | ARG127 |
A | HIS138 |
A | PHE141 |
A | ARG160 |
A | ARG171 |
A | ARG199 |
A | ILE201 |
A | HOH404 |
A | HOH407 |
A | HOH421 |
A | HOH423 |
A | HOH424 |
A | HOH455 |
A | HOH459 |
A | HOH486 |
A | HOH488 |
A | PRO9 |
A | GLY10 |
A | ALA11 |
A | GLY12 |
A | LYS13 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO A 303 |
Chain | Residue |
A | MET6 |
A | GLY7 |
A | LEU8 |
A | ASN175 |
A | MET179 |
A | EDO304 |
A | HOH497 |
A | HOH498 |
A | HOH499 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO A 304 |
Chain | Residue |
A | LEU5 |
A | MET6 |
A | GLY7 |
A | LYS13 |
A | GLY85 |
A | PHE86 |
A | PRO87 |
A | ARG88 |
A | EDO303 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 305 |
Chain | Residue |
A | ASN2 |
A | GLY104 |
A | ARG105 |
A | ARG128 |
A | LEU157 |
A | HOH508 |
A | HOH509 |
Functional Information from PROSITE/UniProt
site_id | PS00113 |
Number of Residues | 12 |
Details | ADENYLATE_KINASE Adenylate kinase signature. FLLDGFPRtvaQ |
Chain | Residue | Details |
A | PHE81-GLN92 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 15 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575 |
Chain | Residue | Details |
A | GLY10 | |
A | THR136 | |
A | CYS150 | |
A | ASP153 | |
A | ARG160 | |
A | ARG171 | |
A | ARG199 | |
A | THR31 | |
A | ARG36 | |
A | GLU57 | |
A | GLY85 | |
A | GLN92 | |
A | ARG127 | |
A | CYS130 | |
A | CYS133 |