5CJT
Isobutyryl-CoA mutase fused with bound adenosylcobalamin, GDP, Mg (holo-IcmF/GDP), and substrate isobutyryl-coenzyme A
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 | 35 |
Details | binding site for residue B12 A 1101 |
Chain | Residue |
A | PHE36 |
A | TYR86 |
A | GLN87 |
A | GLY88 |
A | GLY114 |
A | GLY116 |
A | VAL118 |
A | TYR136 |
A | SER137 |
A | PRO138 |
A | ALA626 |
A | ASP37 |
A | PHE627 |
A | LEU632 |
A | SER650 |
A | GLY741 |
A | GLN742 |
A | THR744 |
A | GLU783 |
A | GLY868 |
A | ARG869 |
A | LEU871 |
A | GLY38 |
A | GLU905 |
A | ALA906 |
A | THR908 |
A | HIS993 |
A | 5AD1102 |
A | CO61103 |
A | HIS39 |
A | ASP40 |
A | ALA41 |
A | SER42 |
A | MET46 |
A | ALA82 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue 5AD A 1102 |
Chain | Residue |
A | PHE598 |
A | GLY600 |
A | TYR779 |
A | GLN865 |
A | GLY868 |
A | HIS899 |
A | ASN901 |
A | GLU905 |
A | THR909 |
A | PRO910 |
A | B121101 |
A | CO61103 |
site_id | AC3 |
Number of Residues | 25 |
Details | binding site for residue CO6 A 1103 |
Chain | Residue |
A | PHE585 |
A | PHE587 |
A | ARG589 |
A | ARG596 |
A | PHE598 |
A | ARG622 |
A | SER624 |
A | SER677 |
A | THR679 |
A | ARG728 |
A | THR730 |
A | GLN732 |
A | GLN742 |
A | TYR772 |
A | TYR779 |
A | HIS780 |
A | SER821 |
A | PHE823 |
A | ARG856 |
A | LYS861 |
A | HIS863 |
A | GLN865 |
A | SER897 |
A | B121101 |
A | 5AD1102 |
site_id | AC4 |
Number of Residues | 17 |
Details | binding site for residue GDP A 1104 |
Chain | Residue |
A | GLY219 |
A | ALA220 |
A | GLY221 |
A | LYS222 |
A | SER223 |
A | SER224 |
A | ARG265 |
A | GLU310 |
A | ASN357 |
A | LYS358 |
A | ASP360 |
A | GLN395 |
A | ALA396 |
A | SER397 |
A | GLU973 |
A | ASN1092 |
A | MG1105 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue MG A 1105 |
Chain | Residue |
A | SER223 |
A | ASP262 |
A | GLU310 |
A | GDP1104 |
A | MG1106 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue MG A 1106 |
Chain | Residue |
A | MG1105 |
A | ILE248 |
A | ASP249 |
A | ASP262 |
A | GLU310 |
A | THR311 |
site_id | AC7 |
Number of Residues | 18 |
Details | binding site for residue B12 B 1101 |
Chain | Residue |
B | HIS39 |
B | ASP40 |
B | ALA41 |
B | SER42 |
B | MET46 |
B | ALA82 |
B | TYR86 |
B | GLN87 |
B | GLY114 |
B | GLY116 |
B | TYR136 |
B | SER137 |
B | PRO138 |
B | GLY141 |
B | MET149 |
B | GLY741 |
B | GLN742 |
B | HIS780 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue CO6 B 1102 |
Chain | Residue |
B | PHE585 |
B | PHE587 |
B | ARG589 |
B | ARG856 |
site_id | AC9 |
Number of Residues | 19 |
Details | binding site for residue GDP B 1103 |
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 | MG1104 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue MG B 1104 |
Chain | Residue |
B | SER223 |
B | ASP262 |
B | GLU310 |
B | GDP1103 |
B | MG1105 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue MG B 1105 |
Chain | Residue |
B | ILE248 |
B | ASP249 |
B | ASP262 |
B | GLU310 |
B | THR311 |
B | MG1104 |
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 | GLY219 | |
A | GLU973 | |
A | ASN1092 | |
B | GLY219 | |
B | SER223 | |
B | ILE248 | |
B | ASP249 | |
B | ASP262 | |
B | ARG265 | |
B | GLU310 | |
B | THR311 | |
A | SER223 | |
B | ASN357 | |
B | GLU973 | |
B | ASN1092 | |
A | ILE248 | |
A | ASP249 | |
A | ASP262 | |
A | ARG265 | |
A | GLU310 | |
A | THR311 | |
A | ASN357 |
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 | PHE587 | |
B | ARG728 | |
B | TYR772 | |
B | SER821 | |
B | ARG856 | |
B | LYS861 | |
A | ARG622 | |
A | ARG728 | |
A | TYR772 | |
A | SER821 | |
A | ARG856 | |
A | LYS861 | |
B | PHE587 | |
B | ARG622 |