5REQ
Methylmalonyl-COA MUTASE, Y89F Mutant, 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 | 47 |
| Details | BINDING SITE FOR RESIDUE B12 A 1800 |
| Chain | Residue |
| A | PHE117 |
| A | GLY333 |
| A | TRP334 |
| A | GLU370 |
| A | ALA371 |
| A | ALA373 |
| A | LEU374 |
| A | GLN454 |
| A | LEU602 |
| A | GLY609 |
| A | HIS610 |
| A | LEU119 |
| A | ASP611 |
| A | ARG612 |
| A | GLY613 |
| A | VAL616 |
| A | ILE617 |
| A | TYR621 |
| A | SER655 |
| A | LEU657 |
| A | GLY659 |
| A | GLY685 |
| A | HIS122 |
| A | GLY686 |
| A | VAL687 |
| A | TYR705 |
| A | THR706 |
| A | THR709 |
| A | SCD1801 |
| A | MCD1802 |
| A | HOH5096 |
| A | HOH5103 |
| A | HOH5108 |
| A | ALA139 |
| A | HOH5144 |
| A | HOH5174 |
| A | HOH5205 |
| A | HOH5280 |
| A | HOH5406 |
| A | HOH5417 |
| A | HOH5443 |
| A | HOH5452 |
| A | VAL206 |
| A | ARG207 |
| A | THR209 |
| A | HIS244 |
| A | GLU247 |
| site_id | AC2 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE SCD A 1801 |
| Chain | Residue |
| A | TYR75 |
| A | THR77 |
| A | MET78 |
| A | ARG82 |
| A | THR85 |
| A | ARG87 |
| A | PHE89 |
| A | SER114 |
| A | SER162 |
| 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 | HIS328 |
| A | GLN330 |
| A | GLN361 |
| A | SER362 |
| A | B121800 |
| A | HOH5005 |
| A | HOH5006 |
| A | HOH5024 |
| A | HOH5033 |
| A | HOH5034 |
| A | HOH5035 |
| A | HOH5066 |
| A | HOH5099 |
| A | HOH5107 |
| A | HOH5119 |
| A | HOH5193 |
| A | HOH5244 |
| A | HOH5490 |
| B | ARG45 |
| site_id | AC3 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE MCD A 1802 |
| Chain | Residue |
| A | ARG207 |
| A | ASN236 |
| A | TYR243 |
| A | HIS244 |
| A | ARG283 |
| A | SER285 |
| A | PHE287 |
| A | THR327 |
| A | HIS328 |
| A | GLN330 |
| A | GLN361 |
| A | SER362 |
| A | B121800 |
| A | HOH5005 |
| A | HOH5006 |
| A | HOH5024 |
| A | HOH5033 |
| A | HOH5034 |
| A | HOH5035 |
| A | HOH5066 |
| A | HOH5099 |
| A | HOH5107 |
| A | HOH5119 |
| A | HOH5193 |
| A | HOH5244 |
| A | HOH5490 |
| B | ARG45 |
| A | TYR75 |
| A | THR77 |
| A | MET78 |
| A | ARG82 |
| A | THR85 |
| A | ARG87 |
| A | PHE89 |
| A | SER114 |
| A | SER164 |
| A | THR166 |
| A | THR195 |
| A | GLN197 |
| site_id | AC4 |
| Number of Residues | 51 |
| Details | BINDING SITE FOR RESIDUE B12 C 2800 |
| Chain | Residue |
| C | PHE117 |
| C | LEU119 |
| C | HIS122 |
| C | ALA139 |
| C | VAL206 |
| C | ARG207 |
| C | THR209 |
| C | TYR243 |
| 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 | SER714 |
| C | SCD2801 |
| C | MCD2802 |
| C | HOH4096 |
| C | HOH4103 |
| C | HOH4108 |
| C | HOH4144 |
| C | HOH4174 |
| C | HOH4205 |
| C | HOH4280 |
| C | HOH4406 |
| C | HOH4417 |
| C | HOH4443 |
| C | HOH4452 |
| site_id | AC5 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE SCD C 2801 |
| Chain | Residue |
| C | TYR75 |
| C | THR77 |
| C | MET78 |
| C | ARG82 |
| C | THR85 |
| C | ARG87 |
| C | PHE89 |
| 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 | HIS328 |
| C | GLN330 |
| C | GLN361 |
| C | SER362 |
| C | B122800 |
| C | HOH4005 |
| C | HOH4006 |
| C | HOH4024 |
| C | HOH4033 |
| C | HOH4034 |
| C | HOH4035 |
| C | HOH4039 |
| C | HOH4066 |
| C | HOH4099 |
| C | HOH4107 |
| C | HOH4119 |
| C | HOH4193 |
| C | HOH4244 |
| C | HOH4490 |
| D | ARG45 |
| site_id | AC6 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE MCD C 2802 |
| Chain | Residue |
| C | TYR75 |
| C | THR77 |
| C | MET78 |
| C | ARG82 |
| C | THR85 |
| C | ARG87 |
| C | PHE89 |
| 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 | HIS328 |
| C | GLN330 |
| C | GLN361 |
| C | SER362 |
| C | B122800 |
| C | HOH4005 |
| C | HOH4006 |
| C | HOH4024 |
| C | HOH4033 |
| C | HOH4034 |
| C | HOH4035 |
| C | HOH4039 |
| C | HOH4066 |
| C | HOH4099 |
| C | HOH4107 |
| C | HOH4119 |
| C | HOH4193 |
| C | HOH4244 |
| C | HOH4490 |
| D | ARG45 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 3001 |
| Chain | Residue |
| B | GLU177 |
| B | VAL216 |
| B | ASP219 |
| B | ARG223 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 3002 |
| Chain | Residue |
| B | THR98 |
| B | ARG100 |
| B | ALA106 |
| B | TRP107 |
| B | GLY354 |
| B | ALA355 |
| B | GLU356 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 3003 |
| Chain | Residue |
| D | GLU177 |
| D | VAL216 |
| D | TRP220 |
| D | ARG223 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 3004 |
| Chain | Residue |
| D | THR98 |
| D | ARG100 |
| D | ALA106 |
| D | TRP107 |
| D | GLY354 |
| D | ALA355 |
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 | PHE89 | |
| 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 | PHE89 | |
| 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 |
