6OXD
Structure of Mycobacterium tuberculosis methylmalonyl-CoA mutase with adenosyl cobalamin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005886 | cellular_component | plasma membrane |
A | 0016853 | molecular_function | isomerase activity |
A | 0016866 | molecular_function | intramolecular transferase activity |
A | 0019678 | biological_process | propionate metabolic process, methylmalonyl pathway |
A | 0031419 | molecular_function | cobalamin binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0009274 | cellular_component | peptidoglycan-based cell wall |
B | 0016853 | molecular_function | isomerase activity |
B | 0016866 | molecular_function | intramolecular transferase activity |
B | 0019652 | biological_process | lactate fermentation to propionate and acetate |
B | 0019678 | biological_process | propionate metabolic process, methylmalonyl pathway |
B | 0031419 | molecular_function | cobalamin binding |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 43 |
Details | binding site for residue B12 A 1000 |
Chain | Residue |
A | TYR105 |
A | GLY349 |
A | TRP350 |
A | LEU352 |
A | GLU386 |
A | ALA387 |
A | ALA389 |
A | LEU390 |
A | GLN470 |
A | GLY628 |
A | HIS629 |
A | PHE133 |
A | ASP630 |
A | ARG631 |
A | GLY632 |
A | GLY672 |
A | SER674 |
A | LEU676 |
A | ALA678 |
A | GLY704 |
A | GLY705 |
A | PHE724 |
A | LEU135 |
A | PRO725 |
A | PRO726 |
A | THR728 |
A | 5AD1001 |
A | NJS1002 |
A | HOH1213 |
A | HOH1219 |
A | HOH1228 |
A | HOH1233 |
A | HOH1317 |
A | HIS138 |
A | HOH1323 |
A | HOH1343 |
A | HOH1359 |
A | HOH1376 |
A | ALA155 |
A | VAL222 |
A | ARG223 |
A | THR225 |
A | GLU263 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue K A 1003 |
Chain | Residue |
A | THR137 |
A | TYR141 |
A | ILE159 |
A | ASP160 |
A | HOH1175 |
site_id | AC3 |
Number of Residues | 49 |
Details | binding site for residues 5AD A 1001 and NJS A 1002 |
Chain | Residue |
A | TYR91 |
A | THR93 |
A | MET94 |
A | ASN97 |
A | GLN98 |
A | THR101 |
A | ARG103 |
A | TYR105 |
A | GLY107 |
A | ALA132 |
A | ALA155 |
A | SER180 |
A | THR182 |
A | THR211 |
A | GLN213 |
A | ARG223 |
A | ASN252 |
A | TYR259 |
A | HIS260 |
A | ARG299 |
A | SER301 |
A | PHE303 |
A | ARG342 |
A | THR343 |
A | HIS344 |
A | GLN346 |
A | GLN377 |
A | SER378 |
A | ASN382 |
A | GLU386 |
A | LEU390 |
A | PRO391 |
A | B121000 |
A | HOH1117 |
A | HOH1144 |
A | HOH1145 |
A | HOH1168 |
A | HOH1174 |
A | HOH1210 |
A | HOH1211 |
A | HOH1212 |
A | HOH1273 |
A | HOH1282 |
A | HOH1301 |
A | HOH1321 |
A | HOH1329 |
A | HOH1339 |
A | HOH1388 |
A | HOH1389 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 25 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P11653 |
Chain | Residue | Details |
A | TYR91 | |
A | GLN213 | |
A | VAL222 | |
A | ARG223 | |
A | HIS260 | |
A | ARG299 | |
A | SER301 | |
A | GLY349 | |
A | GLU386 | |
A | ALA389 | |
A | GLY628 | |
A | MET94 | |
A | ASP630 | |
A | ARG631 | |
A | SER674 | |
A | LEU676 | |
A | GLY705 | |
A | THR728 | |
A | THR101 | |
A | ARG103 | |
A | TYR105 | |
A | SER130 | |
A | PHE133 | |
A | ALA155 | |
A | THR211 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: axial binding residue => ECO:0000250|UniProtKB:P11653 |
Chain | Residue | Details |
A | HIS629 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P11653 |
Chain | Residue | Details |
A | TYR105 |