8DYL
Crystal structure of human methylmalonyl-CoA mutase bound to aquocobalamin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003924 | molecular_function | GTPase activity |
| B | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006790 | biological_process | sulfur compound metabolic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016866 | molecular_function | intramolecular transferase activity |
| B | 0019678 | biological_process | propionate metabolic process, methylmalonyl pathway |
| B | 0031419 | molecular_function | cobalamin binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043547 | biological_process | positive regulation of GTPase activity |
| B | 0044281 | biological_process | small molecule metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050667 | biological_process | homocysteine metabolic process |
| B | 0072341 | molecular_function | modified amino acid binding |
| B | 1901290 | biological_process | succinyl-CoA biosynthetic process |
Functional Information from PROSITE/UniProt
| site_id | PS00544 |
| Number of Residues | 26 |
| Details | METMALONYL_COA_MUTASE Methylmalonyl-CoA mutase signature. RIARNTqiIIqEEsgipKvaDPwGGS |
| Chain | Residue | Details |
| B | ARG403-SER428 |
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 | 15 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20876572","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20876572","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P16332","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P16332","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
