6OXC
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 | 38 |
| Details | binding site for residue B12 A 1000 |
| Chain | Residue |
| A | PHE133 |
| A | GLU386 |
| A | ALA387 |
| A | LEU388 |
| A | ALA389 |
| A | GLN470 |
| A | GLY628 |
| A | HIS629 |
| A | ASP630 |
| A | ARG631 |
| A | GLY632 |
| A | LEU135 |
| A | ILE636 |
| A | SER674 |
| A | LEU676 |
| A | ALA678 |
| A | GLY704 |
| A | GLY705 |
| A | VAL706 |
| A | PHE724 |
| A | PRO725 |
| A | THR728 |
| A | HIS138 |
| A | 5AD1001 |
| A | HOH1119 |
| A | HOH1166 |
| A | HOH1186 |
| A | HOH1191 |
| A | HOH1202 |
| A | HOH1206 |
| A | HOH1338 |
| A | HOH1380 |
| A | ALA155 |
| A | VAL222 |
| A | ARG223 |
| A | THR225 |
| A | GLU263 |
| A | TRP350 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue 5AD A 1001 |
| Chain | Residue |
| A | ALA155 |
| A | GLN346 |
| A | LEU390 |
| A | B121000 |
| A | HOH1120 |
| A | HOH1224 |
| A | HOH1354 |
| A | HOH1517 |
| A | HOH1527 |
| A | HOH1574 |
| A | HOH1593 |
| A | HOH1789 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 132 |
| Details | Domain: {"description":"B12-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00666","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 25 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P11653","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"UniProtKB","id":"P11653","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P11653","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
