3REQ
METHYLMALONYL-COA MUTASE, SUBSTRATE-FREE STATE (POOR QUALITY STRUCTURE)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| 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 | 29 |
| Details | BINDING SITE FOR RESIDUE B12 A 800 |
| Chain | Residue |
| A | LEU119 |
| A | ALA373 |
| A | GLN454 |
| A | ASP608 |
| A | GLY609 |
| A | HIS610 |
| A | ASP611 |
| A | ARG612 |
| A | GLY613 |
| A | ILE617 |
| A | TYR621 |
| A | VAL206 |
| A | GLY653 |
| A | SER655 |
| A | LEU657 |
| A | GLY685 |
| A | GLY686 |
| A | TYR705 |
| A | THR706 |
| A | PRO707 |
| A | THR709 |
| A | ADN801 |
| A | ARG207 |
| A | GLU247 |
| A | GLY333 |
| A | TRP334 |
| A | GLU370 |
| A | ALA371 |
| A | ILE372 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ADN A 801 |
| Chain | Residue |
| A | TYR89 |
| A | TYR243 |
| A | GLU247 |
| A | GLY333 |
| A | TRP334 |
| A | B12800 |
Functional Information from PROSITE/UniProt
| site_id | PS00544 |
| Number of Residues | 26 |
| Details | METMALONYL_COA_MUTASE Methylmalonyl-CoA mutase signature. RIARNTqlFLqQEsgttRviDPwSGS |
| Chain | Residue | Details |
| A | ARG381-SER406 | |
| B | ARG377-SER402 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 131 |
| 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 | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10387043","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4REQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10387043","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8805541","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1REQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4REQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10387043","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8805541","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1REQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4REQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"9772164","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bmt |
| Chain | Residue | Details |
| A | ASP608 | |
| A | HIS661 | |
| A | HIS610 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bmt |
| Chain | Residue | Details |
| B | GLN208 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1bmt |
| Chain | Residue | Details |
| A | ASP608 | |
| A | LYS604 | |
| A | TYR89 | |
| A | HIS244 | |
| A | HIS610 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bmt |
| Chain | Residue | Details |
| A | TYR621 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 62 |
| Chain | Residue | Details |
| A | TYR89 | electrostatic stabiliser, radical stabiliser |
| A | TYR243 | electrostatic stabiliser, radical stabiliser |
| A | HIS244 | electrostatic stabiliser, proton acceptor, proton donor |
| A | LYS604 | electrostatic stabiliser |
| A | ASP608 | electrostatic stabiliser |
| A | HIS610 | metal ligand |
