4REQ
Methylmalonyl-COA Mutase substrate complex
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 | 0016853 | molecular_function | isomerase activity |
| A | 0016866 | molecular_function | intramolecular transferase activity |
| 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 |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0016866 | molecular_function | intramolecular transferase activity |
| C | 0031419 | molecular_function | cobalamin binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0016866 | molecular_function | intramolecular transferase activity |
| D | 0019652 | biological_process | lactate fermentation to propionate and acetate |
| D | 0019678 | biological_process | propionate metabolic process, methylmalonyl pathway |
| D | 0031419 | molecular_function | cobalamin binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 48 |
| Details | BINDING SITE FOR RESIDUE B12 A 800 |
| Chain | Residue |
| A | TYR89 |
| A | GLU247 |
| A | GLY333 |
| A | TRP334 |
| A | LEU336 |
| A | GLU370 |
| A | ALA371 |
| A | ALA373 |
| A | LEU374 |
| A | GLN454 |
| A | LEU602 |
| A | PHE117 |
| A | GLY609 |
| A | HIS610 |
| A | ASP611 |
| A | ARG612 |
| A | GLY613 |
| A | ILE617 |
| A | TYR621 |
| A | SER655 |
| A | LEU657 |
| A | GLY659 |
| A | LEU119 |
| A | GLY685 |
| A | GLY686 |
| A | VAL687 |
| A | TYR705 |
| A | THR706 |
| A | THR709 |
| A | SCA801 |
| A | MCA802 |
| A | 5AD803 |
| A | HOH883 |
| A | HIS122 |
| A | HOH889 |
| A | HOH892 |
| A | HOH914 |
| A | HOH951 |
| A | HOH987 |
| A | HOH1021 |
| A | HOH1025 |
| A | HOH1072 |
| A | HOH1078 |
| A | ALA139 |
| A | VAL206 |
| A | ARG207 |
| A | THR209 |
| A | TYR243 |
| site_id | AC2 |
| Number of Residues | 41 |
| Details | BINDING SITE FOR RESIDUE SCA A 801 |
| Chain | Residue |
| A | TYR75 |
| A | THR77 |
| A | MET78 |
| A | ARG82 |
| A | THR85 |
| A | ARG87 |
| A | TYR89 |
| A | SER114 |
| A | SER164 |
| A | THR166 |
| A | THR195 |
| A | GLN197 |
| A | ARG207 |
| A | ASN236 |
| A | TYR243 |
| A | HIS244 |
| A | ARG283 |
| A | SER285 |
| A | PHE287 |
| A | ARG326 |
| A | THR327 |
| A | HIS328 |
| A | GLN330 |
| A | GLN361 |
| A | SER362 |
| A | B12800 |
| A | HOH807 |
| A | HOH808 |
| A | HOH826 |
| A | HOH835 |
| A | HOH836 |
| A | HOH837 |
| A | HOH865 |
| A | HOH886 |
| A | HOH891 |
| A | HOH900 |
| A | HOH960 |
| A | HOH1028 |
| A | HOH1127 |
| A | HOH1129 |
| B | ARG45 |
| site_id | AC3 |
| Number of Residues | 42 |
| Details | BINDING SITE FOR RESIDUE MCA A 802 |
| Chain | Residue |
| A | THR195 |
| A | GLN197 |
| A | ARG207 |
| A | ASN236 |
| A | TYR243 |
| A | HIS244 |
| A | ARG283 |
| A | SER285 |
| A | PHE287 |
| A | ARG326 |
| A | HIS328 |
| A | GLN330 |
| A | GLN361 |
| A | SER362 |
| A | B12800 |
| A | 5AD803 |
| A | HOH807 |
| A | HOH808 |
| A | HOH826 |
| A | HOH835 |
| A | HOH836 |
| A | HOH837 |
| A | HOH865 |
| A | HOH886 |
| A | HOH891 |
| A | HOH900 |
| A | HOH944 |
| A | HOH960 |
| A | HOH1028 |
| A | HOH1127 |
| A | HOH1129 |
| B | ARG45 |
| A | TYR75 |
| A | THR77 |
| A | MET78 |
| A | ARG82 |
| A | THR85 |
| A | ARG87 |
| A | TYR89 |
| A | SER114 |
| A | SER164 |
| A | THR166 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 5AD A 803 |
| Chain | Residue |
| A | TYR89 |
| A | ALA90 |
| A | GLY91 |
| A | ALA116 |
| A | ALA139 |
| A | GLY140 |
| A | TYR243 |
| A | GLN330 |
| A | ASN366 |
| A | GLU370 |
| A | LEU374 |
| A | B12800 |
| A | MCA802 |
| A | HOH868 |
| A | HOH1074 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1 |
| Chain | Residue |
| A | ALA41 |
| A | GLU42 |
| A | THR251 |
| A | HOH804 |
| A | HOH912 |
| A | HOH915 |
| A | HOH1134 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 639 |
| Chain | Residue |
| B | PHE93 |
| B | THR97 |
| B | ASP316 |
| B | LYS317 |
| B | ARG318 |
| B | GLY319 |
| B | ARG321 |
| site_id | AC7 |
| Number of Residues | 49 |
| Details | BINDING SITE FOR RESIDUE B12 C 800 |
| Chain | Residue |
| C | TYR89 |
| C | PHE117 |
| C | LEU119 |
| C | HIS122 |
| C | ALA139 |
| C | VAL206 |
| C | ARG207 |
| C | THR209 |
| C | HIS244 |
| C | GLU247 |
| C | GLY333 |
| C | TRP334 |
| C | LEU336 |
| C | GLU370 |
| C | ALA371 |
| C | ALA373 |
| C | LEU374 |
| C | GLN454 |
| C | LEU602 |
| C | ASP608 |
| C | GLY609 |
| C | HIS610 |
| C | ASP611 |
| C | ARG612 |
| C | GLY613 |
| C | ILE617 |
| C | TYR621 |
| C | SER655 |
| C | LEU657 |
| C | ALA658 |
| C | GLY659 |
| C | GLY685 |
| C | GLY686 |
| C | VAL687 |
| C | TYR705 |
| C | THR706 |
| C | THR709 |
| C | SCA801 |
| C | MCA802 |
| C | 5AD803 |
| C | HOH881 |
| C | HOH887 |
| C | HOH890 |
| C | HOH949 |
| C | HOH984 |
| C | HOH1018 |
| C | HOH1022 |
| C | HOH1069 |
| C | HOH1075 |
| site_id | AC8 |
| Number of Residues | 42 |
| Details | BINDING SITE FOR RESIDUE SCA C 801 |
| Chain | Residue |
| C | TYR75 |
| C | THR77 |
| C | MET78 |
| C | PHE81 |
| C | ARG82 |
| C | THR85 |
| C | ARG87 |
| C | TYR89 |
| C | SER114 |
| C | SER164 |
| C | THR166 |
| C | THR195 |
| C | GLN197 |
| C | ARG207 |
| C | ASN236 |
| C | TYR243 |
| C | HIS244 |
| C | ARG283 |
| C | SER285 |
| C | PHE287 |
| C | ARG326 |
| C | THR327 |
| C | HIS328 |
| C | GLN330 |
| C | GLN361 |
| C | SER362 |
| C | B12800 |
| C | 5AD803 |
| C | HOH807 |
| C | HOH808 |
| C | HOH826 |
| C | HOH835 |
| C | HOH836 |
| C | HOH837 |
| C | HOH863 |
| C | HOH884 |
| C | HOH889 |
| C | HOH943 |
| C | HOH958 |
| C | HOH1025 |
| C | HOH1123 |
| D | ARG45 |
| site_id | AC9 |
| Number of Residues | 43 |
| Details | BINDING SITE FOR RESIDUE MCA C 802 |
| Chain | Residue |
| C | TYR75 |
| C | THR77 |
| C | MET78 |
| C | PHE81 |
| C | ARG82 |
| C | THR85 |
| C | ARG87 |
| C | TYR89 |
| C | SER114 |
| C | SER164 |
| C | THR166 |
| C | THR195 |
| C | GLN197 |
| C | ARG207 |
| C | ASN236 |
| C | TYR243 |
| C | HIS244 |
| C | ARG283 |
| C | SER285 |
| C | PHE287 |
| C | ARG326 |
| C | THR327 |
| C | HIS328 |
| C | GLN330 |
| C | GLN361 |
| C | SER362 |
| C | B12800 |
| C | 5AD803 |
| C | HOH807 |
| C | HOH808 |
| C | HOH826 |
| C | HOH835 |
| C | HOH836 |
| C | HOH837 |
| C | HOH863 |
| C | HOH884 |
| C | HOH889 |
| C | HOH898 |
| C | HOH943 |
| C | HOH958 |
| C | HOH1025 |
| C | HOH1123 |
| D | ARG45 |
| site_id | BC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 5AD C 803 |
| Chain | Residue |
| C | TYR89 |
| C | ALA90 |
| C | GLY91 |
| C | ALA116 |
| C | ALA139 |
| C | GLY140 |
| C | TYR243 |
| C | GLN330 |
| C | ASN366 |
| C | GLU370 |
| C | LEU374 |
| C | B12800 |
| C | SCA801 |
| C | MCA802 |
| C | HOH866 |
| C | HOH1071 |
| C | HOH1162 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 1 |
| Chain | Residue |
| C | ALA41 |
| C | GLU42 |
| C | HOH804 |
| C | HOH910 |
| C | HOH913 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 639 |
| Chain | Residue |
| D | THR97 |
| D | ASP316 |
| D | LYS317 |
| D | GLY319 |
| D | ARG321 |
Functional Information from PROSITE/UniProt
| site_id | PS00544 |
| Number of Residues | 26 |
| Details | METMALONYL_COA_MUTASE Methylmalonyl-CoA mutase signature. RIARNTgiVLaEEvnigRvnDPaGGS |
| Chain | Residue | Details |
| B | ARG377-SER402 | |
| A | ARG381-SER406 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10387043, ECO:0007744|PDB:4REQ |
| Chain | Residue | Details |
| A | ALA76 | |
| A | MET245 | |
| A | LEU284 | |
| A | PHE286 | |
| C | ALA76 | |
| C | TYR79 | |
| C | PRO83 | |
| C | ILE86 | |
| C | GLN88 | |
| C | ALA90 | |
| C | VAL115 | |
| A | TYR79 | |
| C | ILE196 | |
| C | ASN198 | |
| C | MET245 | |
| C | LEU284 | |
| C | PHE286 | |
| A | PRO83 | |
| A | ILE86 | |
| A | GLN88 | |
| A | ALA90 | |
| A | VAL115 | |
| A | ILE196 | |
| A | ASN198 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10387043, ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ, ECO:0007744|PDB:4REQ |
| Chain | Residue | Details |
| A | ASP118 | |
| A | GLY613 | |
| A | SER656 | |
| A | ALA658 | |
| A | VAL687 | |
| A | VAL710 | |
| C | ASP118 | |
| C | GLY140 | |
| C | ARG207 | |
| C | ASN208 | |
| C | TRP334 | |
| A | GLY140 | |
| C | ALA371 | |
| C | LEU374 | |
| C | HIS610 | |
| C | ARG612 | |
| C | GLY613 | |
| C | SER656 | |
| C | ALA658 | |
| C | VAL687 | |
| C | VAL710 | |
| A | ARG207 | |
| A | ASN208 | |
| A | TRP334 | |
| A | ALA371 | |
| A | LEU374 | |
| A | HIS610 | |
| A | ARG612 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:10387043, ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ, ECO:0007744|PDB:4REQ |
| Chain | Residue | Details |
| A | ASP611 | |
| C | ASP611 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:9772164 |
| Chain | Residue | Details |
| A | ALA90 | |
| C | ALA90 |
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 | 3 |
| Details | Annotated By Reference To The Literature 1bmt |
| Chain | Residue | Details |
| C | ASP608 | |
| C | HIS661 | |
| C | HIS610 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bmt |
| Chain | Residue | Details |
| B | GLN208 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bmt |
| Chain | Residue | Details |
| D | GLN208 |
| site_id | CSA5 |
| 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 | CSA6 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1bmt |
| Chain | Residue | Details |
| C | ASP608 | |
| C | LYS604 | |
| C | TYR89 | |
| C | HIS244 | |
| C | HIS610 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bmt |
| Chain | Residue | Details |
| A | TYR621 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bmt |
| Chain | Residue | Details |
| C | TYR621 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 62 |
| Chain | Residue | Details |
| A | ALA90 | electrostatic stabiliser, radical stabiliser |
| A | HIS244 | electrostatic stabiliser, radical stabiliser |
| A | MET245 | electrostatic stabiliser, proton acceptor, proton donor |
| A | MET605 | electrostatic stabiliser |
| A | GLY609 | electrostatic stabiliser |
| A | ASP611 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 62 |
| Chain | Residue | Details |
| C | ALA90 | electrostatic stabiliser, radical stabiliser |
| C | HIS244 | electrostatic stabiliser, radical stabiliser |
| C | MET245 | electrostatic stabiliser, proton acceptor, proton donor |
| C | MET605 | electrostatic stabiliser |
| C | GLY609 | electrostatic stabiliser |
| C | ASP611 | metal ligand |
