4XC8
Isobutyryl-CoA mutase fused with bound butyryl-CoA, GDP, and Mg and without cobalamin (apo-IcmF/GDP)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
| A | 0005525 | molecular_function | GTP binding |
| A | 0006637 | biological_process | acyl-CoA metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016866 | molecular_function | intramolecular transferase activity |
| A | 0031419 | molecular_function | cobalamin binding |
| A | 0034784 | molecular_function | pivalyl-CoA mutase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047727 | molecular_function | isobutyryl-CoA mutase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003924 | molecular_function | GTPase activity |
| B | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
| B | 0005525 | molecular_function | GTP binding |
| B | 0006637 | biological_process | acyl-CoA metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016866 | molecular_function | intramolecular transferase activity |
| B | 0031419 | molecular_function | cobalamin binding |
| B | 0034784 | molecular_function | pivalyl-CoA mutase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047727 | molecular_function | isobutyryl-CoA mutase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue BCO A 1101 |
| Chain | Residue |
| A | PHE585 |
| A | THR730 |
| A | GLN732 |
| A | TYR772 |
| A | HIS780 |
| A | SER821 |
| A | PHE823 |
| A | ARG856 |
| A | LYS861 |
| A | TYR862 |
| A | HIS863 |
| A | PHE587 |
| A | GLN865 |
| A | SER897 |
| A | ARG589 |
| A | ARG596 |
| A | PHE598 |
| A | ARG622 |
| A | SER677 |
| A | THR679 |
| A | ARG728 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue GDP A 1102 |
| Chain | Residue |
| A | GLY219 |
| A | ALA220 |
| A | GLY221 |
| A | LYS222 |
| A | SER223 |
| A | SER224 |
| A | ASP262 |
| A | ARG265 |
| A | GLU310 |
| A | ASN357 |
| A | LYS358 |
| A | ASP360 |
| A | GLN395 |
| A | ALA396 |
| A | SER397 |
| A | GLU973 |
| A | ASN1092 |
| A | MG1103 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 1103 |
| Chain | Residue |
| A | SER223 |
| A | ASP262 |
| A | GLU310 |
| A | GDP1102 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 1104 |
| Chain | Residue |
| A | ILE248 |
| A | ASP249 |
| A | ASP262 |
| A | GLU310 |
| A | THR311 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue BCO B 1101 |
| Chain | Residue |
| B | PHE585 |
| B | PHE587 |
| B | TYR772 |
| B | SER821 |
| B | ASN896 |
| B | SER897 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | binding site for residue GDP B 1102 |
| Chain | Residue |
| B | GLY219 |
| B | ALA220 |
| B | GLY221 |
| B | LYS222 |
| B | SER223 |
| B | SER224 |
| B | ARG265 |
| B | GLU310 |
| B | ALA338 |
| B | GLN341 |
| B | ASN357 |
| B | LYS358 |
| B | ASP360 |
| B | GLN395 |
| B | ALA396 |
| B | SER397 |
| B | GLU973 |
| B | ASN1092 |
| B | MG1103 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 1103 |
| Chain | Residue |
| B | SER223 |
| B | GLY261 |
| B | ASP262 |
| B | GLU310 |
| B | LYS344 |
| B | GDP1102 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 1104 |
| Chain | Residue |
| B | ILE248 |
| B | ASP249 |
| B | ASP262 |
| B | GLU310 |
| B | THR311 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue => ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000269|PubMed:25675500, ECO:0007744|PDB:4XC6 |
| Chain | Residue | Details |
| A | HIS39 | |
| B | HIS39 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000269|PubMed:25675500, ECO:0007744|PDB:4XC6 |
| Chain | Residue | Details |
| A | ILE248 | |
| A | ASP249 | |
| A | ASP262 | |
| A | ARG265 | |
| A | GLU310 | |
| A | THR311 | |
| A | ASN357 | |
| A | GLU973 | |
| A | ASN1092 | |
| B | GLY219 | |
| B | SER223 | |
| B | ILE248 | |
| B | ASP249 | |
| B | ASP262 | |
| B | ARG265 | |
| B | GLU310 | |
| B | THR311 | |
| B | ASN357 | |
| B | GLU973 | |
| B | ASN1092 | |
| A | GLY219 | |
| A | SER223 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02050, ECO:0000269|PubMed:25675500 |
| Chain | Residue | Details |
| A | ARG728 | |
| A | TYR772 | |
| A | SER821 | |
| A | ARG856 | |
| A | LYS861 | |
| B | PHE587 | |
| B | ARG622 | |
| B | ARG728 | |
| B | TYR772 | |
| B | SER821 | |
| B | ARG856 | |
| B | LYS861 | |
| A | PHE587 | |
| A | ARG622 |
