3TW7
Structure of Rhizobium etli pyruvate carboxylase T882A crystallized without acetyl coenzyme-A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004075 | molecular_function | biotin carboxylase activity |
| A | 0004736 | molecular_function | pyruvate carboxylase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006090 | biological_process | pyruvate metabolic process |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004075 | molecular_function | biotin carboxylase activity |
| B | 0004736 | molecular_function | pyruvate carboxylase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006090 | biological_process | pyruvate metabolic process |
| B | 0006094 | biological_process | gluconeogenesis |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 1200 |
| Chain | Residue |
| A | MET534 |
| A | ARG535 |
| A | GLU537 |
| A | ASP768 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1201 |
| Chain | Residue |
| A | ASP549 |
| A | KCX718 |
| A | HIS747 |
| A | HIS749 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1202 |
| Chain | Residue |
| A | LYS989 |
| A | VAL990 |
| A | TYR987 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 1200 |
| Chain | Residue |
| B | MET534 |
| B | ARG535 |
| B | GLU537 |
| B | ASP768 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1201 |
| Chain | Residue |
| B | ASP549 |
| B | KCX718 |
| B | HIS747 |
| B | HIS749 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1202 |
| Chain | Residue |
| B | TYR987 |
| B | PRO988 |
| B | LYS989 |
| B | VAL990 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 11 |
| Details | M-CSA 223 |
| Chain | Residue | Details |
| A | GLU283 | metal ligand |
| A | GLY753 | metal ligand |
| A | LYS886 | proton acceptor, proton donor, proton relay |
| A | GLU297 | metal ligand |
| A | ASN299 | metal ligand |
| A | GLU305 | electrostatic stabiliser, proton acceptor, proton donor |
| A | ARG353 | activator, electrostatic stabiliser |
| A | ASP549 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| A | ASP655 | activator, metal ligand |
| A | KCX718 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | THR751 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 11 |
| Details | M-CSA 223 |
| Chain | Residue | Details |
| B | GLU283 | metal ligand |
| B | GLY753 | metal ligand |
| B | LYS886 | proton acceptor, proton donor, proton relay |
| B | GLU297 | metal ligand |
| B | ASN299 | metal ligand |
| B | GLU305 | electrostatic stabiliser, proton acceptor, proton donor |
| B | ARG353 | activator, electrostatic stabiliser |
| B | ASP549 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| B | ASP655 | activator, metal ligand |
| B | KCX718 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | THR751 | metal ligand |
