Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004474 | molecular_function | malate synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006097 | biological_process | glyoxylate cycle |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0009436 | biological_process | glyoxylate catabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004474 | molecular_function | malate synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006097 | biological_process | glyoxylate cycle |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0009436 | biological_process | glyoxylate catabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1000 |
| Chain | Residue |
| A | GLU427 |
| A | ASP455 |
| A | PYR810 |
| A | HOH2222 |
| A | HOH2253 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1001 |
| Chain | Residue |
| B | HOH2230 |
| B | GLU427 |
| B | ASP455 |
| B | PYR910 |
| B | HOH2223 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ACO A 800 |
| Chain | Residue |
| A | VAL118 |
| A | VAL119 |
| A | PRO120 |
| A | ARG125 |
| A | TYR126 |
| A | ASN129 |
| A | ALA130 |
| A | ASP273 |
| A | SER274 |
| A | ARG311 |
| A | ARG338 |
| A | MET508 |
| A | PRO536 |
| A | PRO538 |
| A | CSO617 |
| A | MET629 |
| A | ASP631 |
| A | ALA633 |
| A | PYR810 |
| A | HOH2222 |
| A | HOH2338 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ACO B 900 |
| Chain | Residue |
| B | VAL118 |
| B | VAL119 |
| B | ARG125 |
| B | TYR126 |
| B | ASN129 |
| B | ALA130 |
| B | SER274 |
| B | ARG311 |
| B | ARG338 |
| B | LEU454 |
| B | MET508 |
| B | TRP534 |
| B | PRO536 |
| B | PRO538 |
| B | CSO617 |
| B | LYS619 |
| B | MET629 |
| B | ASP631 |
| B | ALA633 |
| B | PYR910 |
| B | HOH2223 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PYR A 810 |
| Chain | Residue |
| A | ARG338 |
| A | GLU427 |
| A | GLY452 |
| A | PHE453 |
| A | LEU454 |
| A | ASP455 |
| A | TRP534 |
| A | ALA633 |
| A | ACO800 |
| A | MG1000 |
| A | HOH2171 |
| A | HOH2222 |
| A | HOH2253 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PYR B 910 |
| Chain | Residue |
| B | ARG338 |
| B | GLU427 |
| B | GLY452 |
| B | PHE453 |
| B | LEU454 |
| B | ASP455 |
| B | TRP534 |
| B | ACO900 |
| B | MG1001 |
| B | HOH2223 |
| B | HOH2224 |
| B | HOH2230 |
| B | HOH2248 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PG4 B 1002 |
| Chain | Residue |
| B | THR110 |
| B | SER111 |
| B | GLN112 |
| B | ASN234 |
| B | GLY235 |
| B | GLY500 |
| B | ASN552 |
| B | GLN554 |
| B | HOH2279 |
| B | HOH2315 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PG4 B 1003 |
| Chain | Residue |
| B | LEU433 |
| B | ARG436 |
| B | ASN488 |
| B | ASN566 |
| B | PHE569 |
| B | GLU570 |
| B | LEU573 |
| B | HOH2121 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 1001 |
| Chain | Residue |
| A | HOH2448 |
| A | THR110 |
| A | SER111 |
| A | GLN554 |
Functional Information from PROSITE/UniProt
| site_id | PS00589 |
| Number of Residues | 16 |
| Details | PTS_HPR_SER PTS HPR domain serine phosphorylation site signature. EIsLHgRSLLFIRnVG |
| Chain | Residue | Details |
| A | GLU326-GLY341 | |
| B | GLU326-GLY341 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| B | ASN339 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| B | ARG632 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | VAL119 | |
| B | TYR126 | |
| B | VAL275 | |
| B | LYS312 | |
| B | ASN339 | |
| B | GLU428 | |
| B | PHE453 | |
| B | ARG456 | |
| B | SER537 | |
| Chain | Residue | Details |
| B | SER618 | |
| B | ALA689 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1d8c |
| Chain | Residue | Details |
| A | ARG338 | |
| A | GLU272 | |
| A | ASP270 | |
| A | ASP631 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1d8c |
| Chain | Residue | Details |
| B | ARG338 | |
| B | GLU272 | |
| B | ASP270 | |
| B | ASP631 | |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 53 |
| Chain | Residue | Details |
| B | CYS271 | electrostatic stabiliser, hydrogen bond acceptor |
| B | ASP273 | electrostatic stabiliser, hydrogen bond acceptor |
| B | ASN339 | electrostatic stabiliser, hydrogen bond donor |
| B | GLU428 | metal ligand |
| B | ARG456 | metal ligand |
| B | ARG632 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
