Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004611 | molecular_function | phosphoenolpyruvate carboxykinase activity |
A | 0004612 | molecular_function | phosphoenolpyruvate carboxykinase (ATP) activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006094 | biological_process | gluconeogenesis |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0017076 | molecular_function | purine nucleotide binding |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 998 |
Chain | Residue |
A | LYS213 |
A | HIS232 |
A | ASP269 |
A | ATP541 |
A | HOH777 |
A | HOH801 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 999 |
Chain | Residue |
A | HOH619 |
A | HOH776 |
A | THR255 |
A | ATP541 |
A | HOH605 |
site_id | AC3 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE ATP A 541 |
Chain | Residue |
A | HIS232 |
A | LEU249 |
A | SER250 |
A | GLY251 |
A | THR252 |
A | GLY253 |
A | LYS254 |
A | THR255 |
A | THR256 |
A | ASP269 |
A | LYS288 |
A | GLU297 |
A | ARG333 |
A | ARG449 |
A | ILE450 |
A | SER451 |
A | ILE452 |
A | THR455 |
A | HOH605 |
A | HOH619 |
A | HOH624 |
A | HOH743 |
A | HOH777 |
A | MN998 |
A | MG999 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CO2 A 542 |
Chain | Residue |
A | ARG65 |
A | TYR207 |
A | LYS213 |
A | HOH801 |
A | HOH815 |
A | HOH839 |
Functional Information from PROSITE/UniProt
site_id | PS00532 |
Number of Residues | 16 |
Details | PEPCK_ATP Phosphoenolpyruvate carboxykinase (ATP) signature. LIGDDEHgWdDdGVfN |
Chain | Residue | Details |
A | LEU265-ASN280 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ARG65 | |
A | TYR207 | |
A | LYS213 | |
A | ARG333 | |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | LYS149 | |
A | ASN150 | |
A | PHE152 | |
A | GLY283 | |
Chain | Residue | Details |
A | HIS232 | |
A | ASP269 | |
Chain | Residue | Details |
A | GLY248 | |
A | GLU297 | |
A | ARG449 | |
A | THR455 | |
Chain | Residue | Details |
A | LYS87 | |
A | LYS523 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1aq2 |
Chain | Residue | Details |
A | LYS254 | |
A | ARG333 | |
A | HIS232 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1aq2 |
Chain | Residue | Details |
A | ARG333 | |
A | HIS232 | |
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 51 |
Chain | Residue | Details |
A | ARG65 | electrostatic stabiliser, increase electrophilicity |
A | LYS213 | metal ligand |
A | HIS232 | electrostatic stabiliser, hydrogen bond donor, metal ligand |
A | SER250 | steric role |
A | LYS254 | electrostatic stabiliser, hydrogen bond donor |
A | THR255 | metal ligand |
A | ASP269 | metal ligand |
A | ARG333 | electrostatic stabiliser, hydrogen bond donor |