4QBI
Crystal structure of a stable adenylate kinase variant AKlse6
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 | 0008270 | molecular_function | zinc ion binding |
| 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 |
| 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 | 0008270 | molecular_function | zinc ion binding |
| 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 | 0046872 | molecular_function | metal ion binding |
| 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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 301 |
| Chain | Residue |
| A | CYS130 |
| A | CYS133 |
| A | CYS150 |
| A | CYS153 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 302 |
| Chain | Residue |
| A | HOH678 |
| A | AP5303 |
| A | HOH674 |
| A | HOH675 |
| A | HOH676 |
| A | HOH677 |
| site_id | AC3 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE AP5 A 303 |
| Chain | Residue |
| A | LEU8 |
| A | PRO9 |
| A | GLY10 |
| A | ALA11 |
| A | GLY12 |
| A | LYS13 |
| A | GLY14 |
| A | THR15 |
| A | THR31 |
| A | GLY32 |
| A | ARG36 |
| A | MET53 |
| A | ASP57 |
| A | LEU58 |
| A | VAL59 |
| A | GLY85 |
| A | PHE86 |
| A | ARG88 |
| A | GLN92 |
| A | ARG123 |
| A | ARG127 |
| A | THR136 |
| A | TYR137 |
| A | HIS138 |
| A | PHE141 |
| A | ARG160 |
| A | ARG171 |
| A | GLY197 |
| A | GLN199 |
| A | ILE201 |
| A | MG302 |
| A | HOH413 |
| A | HOH425 |
| A | HOH428 |
| A | HOH440 |
| A | HOH483 |
| A | HOH515 |
| A | HOH675 |
| A | HOH676 |
| A | HOH678 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 301 |
| Chain | Residue |
| B | CYS130 |
| B | CYS133 |
| B | CYS150 |
| B | CYS153 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 302 |
| Chain | Residue |
| B | AP5303 |
| B | HOH652 |
| B | HOH653 |
| B | HOH654 |
| B | HOH655 |
| site_id | AC6 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE AP5 B 303 |
| Chain | Residue |
| B | PRO9 |
| B | GLY10 |
| B | ALA11 |
| B | GLY12 |
| B | LYS13 |
| B | GLY14 |
| B | THR15 |
| B | THR31 |
| B | GLY32 |
| B | ARG36 |
| B | ASP57 |
| B | VAL59 |
| B | THR64 |
| B | GLY85 |
| B | PHE86 |
| B | ARG88 |
| B | GLN92 |
| B | ARG123 |
| B | ARG127 |
| B | THR136 |
| B | TYR137 |
| B | HIS138 |
| B | PHE141 |
| B | ARG160 |
| B | ARG171 |
| B | GLN199 |
| B | ILE201 |
| B | MG302 |
| B | HOH410 |
| B | HOH412 |
| B | HOH427 |
| B | HOH437 |
| B | HOH440 |
| B | HOH462 |
| B | HOH652 |
| B | HOH654 |
| B | HOH655 |
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 | 30 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:9715904 |
| Chain | Residue | Details |
| A | GLY10 | |
| A | THR136 | |
| A | CYS150 | |
| A | CYS153 | |
| A | ARG160 | |
| A | ARG171 | |
| A | GLN199 | |
| B | GLY10 | |
| B | THR31 | |
| B | ARG36 | |
| B | ASP57 | |
| A | THR31 | |
| B | GLY85 | |
| B | GLN92 | |
| B | ARG127 | |
| B | CYS130 | |
| B | CYS133 | |
| B | THR136 | |
| B | CYS150 | |
| B | CYS153 | |
| B | ARG160 | |
| B | ARG171 | |
| A | ARG36 | |
| B | GLN199 | |
| A | ASP57 | |
| A | GLY85 | |
| A | GLN92 | |
| A | ARG127 | |
| A | CYS130 | |
| A | CYS133 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 290 |
| Chain | Residue | Details |
| A | LYS13 | electrostatic stabiliser |
| A | ARG88 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| A | ARG127 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| A | ARG160 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| A | ARG171 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 290 |
| Chain | Residue | Details |
| B | LYS13 | electrostatic stabiliser |
| B | ARG88 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| B | ARG127 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| B | ARG160 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| B | ARG171 | electrostatic stabiliser |
