6YBQ
Engineered glycolyl-CoA carboxylase (quintuple mutant) with bound CoA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| A | 0016874 | molecular_function | ligase activity |
| B | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| B | 0016874 | molecular_function | ligase activity |
| C | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| C | 0016874 | molecular_function | ligase activity |
| D | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| D | 0016874 | molecular_function | ligase activity |
| E | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| E | 0016874 | molecular_function | ligase activity |
| F | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| F | 0016874 | molecular_function | ligase activity |
| G | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| G | 0005524 | molecular_function | ATP binding |
| G | 0016042 | biological_process | lipid catabolic process |
| G | 0016874 | molecular_function | ligase activity |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| H | 0005524 | molecular_function | ATP binding |
| H | 0016042 | biological_process | lipid catabolic process |
| H | 0016874 | molecular_function | ligase activity |
| H | 0046872 | molecular_function | metal ion binding |
| I | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| I | 0005524 | molecular_function | ATP binding |
| I | 0016042 | biological_process | lipid catabolic process |
| I | 0016874 | molecular_function | ligase activity |
| I | 0046872 | molecular_function | metal ion binding |
| J | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| J | 0005524 | molecular_function | ATP binding |
| J | 0016042 | biological_process | lipid catabolic process |
| J | 0016874 | molecular_function | ligase activity |
| J | 0046872 | molecular_function | metal ion binding |
| K | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| K | 0005524 | molecular_function | ATP binding |
| K | 0016042 | biological_process | lipid catabolic process |
| K | 0016874 | molecular_function | ligase activity |
| K | 0046872 | molecular_function | metal ion binding |
| L | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| L | 0005524 | molecular_function | ATP binding |
| L | 0016042 | biological_process | lipid catabolic process |
| L | 0016874 | molecular_function | ligase activity |
| L | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue COA A 601 |
| Chain | Residue |
| A | ARG23 |
| A | GLY97 |
| A | GLY129 |
| A | ALA131 |
| A | ARG132 |
| A | ILE133 |
| A | GLN134 |
| A | TYR189 |
| B | ARG441 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue COA B 601 |
| Chain | Residue |
| A | ILE438 |
| A | ARG441 |
| B | ARG23 |
| B | PHE93 |
| B | PHE96 |
| B | GLY97 |
| B | GLY129 |
| B | ALA131 |
| B | ARG132 |
| B | ILE133 |
| B | GLN134 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue COA C 601 |
| Chain | Residue |
| C | ARG23 |
| C | GLY97 |
| C | GLY129 |
| C | ALA131 |
| C | ARG132 |
| C | ILE133 |
| D | ARG441 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue COA D 601 |
| Chain | Residue |
| C | ARG441 |
| D | ARG23 |
| D | GLY97 |
| D | GLY129 |
| D | ALA131 |
| D | ARG132 |
| D | ILE133 |
| D | GLN134 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue COA E 601 |
| Chain | Residue |
| E | ARG23 |
| E | GLY97 |
| E | GLY129 |
| E | ALA131 |
| E | ARG132 |
| E | ILE133 |
| E | GLN134 |
| E | TYR189 |
| E | ASP196 |
| F | ARG441 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue COA F 601 |
| Chain | Residue |
| E | ARG441 |
| F | ARG23 |
| F | GLY97 |
| F | GLY129 |
| F | ALA131 |
| F | ARG132 |
| F | ILE133 |
| F | ASP196 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for Di-peptide BTI G 701 and LYS G 633 |
| Chain | Residue |
| A | ASN278 |
| A | PRO362 |
| A | GLY363 |
| A | PHE364 |
| A | HOH731 |
| G | GLU630 |
| G | ALA631 |
| G | MET632 |
| G | MET634 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for Di-peptide BTI H 701 and LYS H 633 |
| Chain | Residue |
| C | ASN278 |
| C | PHE364 |
| H | ALA631 |
| H | MET632 |
| H | MET634 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide BTI I 701 and LYS I 633 |
| Chain | Residue |
| E | ASN278 |
| E | VAL332 |
| E | PHE364 |
| I | ALA631 |
| I | MET632 |
| I | MET634 |
| I | HOH807 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide BTI J 701 and LYS J 633 |
| Chain | Residue |
| B | ASN278 |
| B | VAL332 |
| B | PHE364 |
| J | GLU630 |
| J | ALA631 |
| J | MET632 |
| J | MET634 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide BTI K 701 and LYS K 633 |
| Chain | Residue |
| F | ASN278 |
| F | PHE364 |
| K | GLU630 |
| K | ALA631 |
| K | MET632 |
| K | MET634 |
| K | HOH804 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for Di-peptide BTI L 701 and LYS L 633 |
| Chain | Residue |
| D | ASN278 |
| D | PHE364 |
| L | GLU630 |
| L | ALA631 |
| L | MET632 |
| L | MET634 |
Functional Information from PROSITE/UniProt
| site_id | PS00188 |
| Number of Residues | 18 |
| Details | BIOTIN Biotin-requiring enzymes attachment site. GEpLaiVeAMKMenvLrA |
| Chain | Residue | Details |
| G | GLY623-ALA640 |
| site_id | PS00866 |
| Number of Residues | 15 |
| Details | CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVMIKASaggGGkG |
| Chain | Residue | Details |
| G | TYR153-GLY167 |
| site_id | PS00867 |
| Number of Residues | 8 |
| Details | CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FLEMNTRL |
| Chain | Residue | Details |
| G | PHE286-LEU293 |
