3SK3
Crystal structure of Salmonella typhimurium acetate kinase (AckA) with citrate bound at the dimeric interface
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006082 | biological_process | organic acid metabolic process |
A | 0006083 | biological_process | acetate metabolic process |
A | 0006085 | biological_process | acetyl-CoA biosynthetic process |
A | 0008776 | molecular_function | acetate kinase activity |
A | 0008980 | molecular_function | propionate kinase activity |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0016774 | molecular_function | phosphotransferase activity, carboxyl group as acceptor |
A | 0046872 | molecular_function | metal ion binding |
A | 0047900 | molecular_function | formate kinase activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006082 | biological_process | organic acid metabolic process |
B | 0006083 | biological_process | acetate metabolic process |
B | 0006085 | biological_process | acetyl-CoA biosynthetic process |
B | 0008776 | molecular_function | acetate kinase activity |
B | 0008980 | molecular_function | propionate kinase activity |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
B | 0016774 | molecular_function | phosphotransferase activity, carboxyl group as acceptor |
B | 0046872 | molecular_function | metal ion binding |
B | 0047900 | molecular_function | formate kinase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE CIT A 501 |
Chain | Residue |
A | ARG178 |
A | HOH478 |
A | HOH538 |
A | HOH620 |
B | ARG309 |
B | LYS312 |
B | HOH552 |
B | HOH608 |
A | ASP257 |
A | THR258 |
A | LEU259 |
A | GLY260 |
A | TYR313 |
A | HOH422 |
A | HOH452 |
A | HOH470 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 601 |
Chain | Residue |
A | TYR188 |
A | GLN191 |
A | GLU192 |
A | GLN393 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 604 |
Chain | Residue |
A | GLY367 |
A | LYS368 |
A | SER369 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 602 |
Chain | Residue |
B | PHE187 |
B | GLU192 |
B | LYS195 |
B | GLN393 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 603 |
Chain | Residue |
B | VAL148 |
B | PHE149 |
B | PHE153 |
B | THR184 |
B | PHE187 |
B | ASP394 |
B | HOH415 |
B | HOH420 |
Functional Information from PROSITE/UniProt
site_id | PS01075 |
Number of Residues | 12 |
Details | ACETATE_KINASE_1 Acetate and butyrate kinases family signature 1. VLvLNcGSSSlK |
Chain | Residue | Details |
A | VAL6-LYS17 |
site_id | PS01076 |
Number of Residues | 18 |
Details | ACETATE_KINASE_2 Acetate and butyrate kinases family signature 2. IItcHlGnGgSVsAirnG |
Chain | Residue | Details |
A | ILE206-GLY223 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00020 |
Chain | Residue | Details |
A | ASP150 | |
B | ASP150 |
site_id | SWS_FT_FI2 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00020 |
Chain | Residue | Details |
A | ARG91 | |
A | HIS210 | |
A | ASP285 | |
A | GLY333 | |
A | GLU387 | |
B | ASN10 | |
B | LYS17 | |
B | ARG91 | |
B | HIS210 | |
B | ASP285 | |
B | GLY333 | |
B | GLU387 | |
A | ASN10 | |
A | LYS17 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00020 |
Chain | Residue | Details |
B | HIS182 | |
A | HIS182 | |
A | ARG243 | |
B | ARG243 |