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 | 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 |
C | 0003824 | molecular_function | catalytic activity |
C | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0016853 | molecular_function | isomerase activity |
C | 0016866 | molecular_function | intramolecular transferase activity |
C | 0019678 | biological_process | propionate metabolic process, methylmalonyl pathway |
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. RIARNTqlFLqQEsgttRviDPwSGS |
Chain | Residue | Details |
A | ARG381-SER406 | |
B | ARG377-SER402 |
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 |