1ON9
Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with hydrolyzed methylmalonyl-coenzyme a bound)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| A | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016874 | molecular_function | ligase activity |
| A | 0047154 | molecular_function | methylmalonyl-CoA carboxytransferase activity |
| B | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| B | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016874 | molecular_function | ligase activity |
| B | 0047154 | molecular_function | methylmalonyl-CoA carboxytransferase activity |
| C | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| C | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| C | 0006633 | biological_process | fatty acid biosynthetic process |
| C | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016874 | molecular_function | ligase activity |
| C | 0047154 | molecular_function | methylmalonyl-CoA carboxytransferase activity |
| D | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| D | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| D | 0006633 | biological_process | fatty acid biosynthetic process |
| D | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016874 | molecular_function | ligase activity |
| D | 0047154 | molecular_function | methylmalonyl-CoA carboxytransferase activity |
| E | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| E | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| E | 0006633 | biological_process | fatty acid biosynthetic process |
| E | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| E | 0016740 | molecular_function | transferase activity |
| E | 0016874 | molecular_function | ligase activity |
| E | 0047154 | molecular_function | methylmalonyl-CoA carboxytransferase activity |
| F | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| F | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| F | 0006633 | biological_process | fatty acid biosynthetic process |
| F | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| F | 0016740 | molecular_function | transferase activity |
| F | 0016874 | molecular_function | ligase activity |
| F | 0047154 | molecular_function | methylmalonyl-CoA carboxytransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CD A 7001 |
| Chain | Residue |
| A | HIS388 |
| A | HOH7006 |
| A | HOH7009 |
| A | HOH7407 |
| D | HIS388 |
| D | HOH4368 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CD B 7002 |
| Chain | Residue |
| E | HIS388 |
| E | HOH4466 |
| E | HOH4468 |
| B | HIS388 |
| B | HOH7010 |
| B | HOH7252 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CD C 7003 |
| Chain | Residue |
| C | HIS388 |
| C | HOH7009 |
| C | HOH7010 |
| F | HIS388 |
| F | HOH6008 |
| F | HOH6258 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MCA A 4001 |
| Chain | Residue |
| A | ARG34 |
| A | ARG35 |
| A | PHE105 |
| A | MET108 |
| A | GLY109 |
| A | SER111 |
| A | GLY141 |
| A | ALA143 |
| A | HOH7158 |
| A | HOH7535 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MCA B 4002 |
| Chain | Residue |
| B | ARG35 |
| B | MET108 |
| B | GLY109 |
| B | SER111 |
| B | ALA143 |
| B | HOH7215 |
| B | HOH7351 |
| B | HOH7359 |
| B | HOH7416 |
| B | HOH7499 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MCA C 4003 |
| Chain | Residue |
| C | ARG34 |
| C | ARG35 |
| C | LYS38 |
| C | PHE105 |
| C | MET108 |
| C | GLY109 |
| C | SER111 |
| C | GLY141 |
| C | ALA143 |
| C | HOH7148 |
| C | HOH7494 |
| C | HOH7535 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MCA D 4004 |
| Chain | Residue |
| D | ARG34 |
| D | ARG35 |
| D | LYS38 |
| D | PHE105 |
| D | MET108 |
| D | GLY109 |
| D | SER111 |
| D | GLY141 |
| D | ALA143 |
| D | HOH4240 |
| D | HOH4282 |
| D | HOH4361 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE MCA E 4005 |
| Chain | Residue |
| A | HOH7494 |
| E | ARG34 |
| E | ARG35 |
| E | LYS38 |
| E | MET108 |
| E | GLY109 |
| E | SER111 |
| E | GLY141 |
| E | ALA143 |
| E | HOH4140 |
| E | HOH4384 |
| E | HOH4494 |
| E | HOH4515 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE MCA F 4006 |
| Chain | Residue |
| F | ARG34 |
| F | ARG35 |
| F | LYS38 |
| F | PHE105 |
| F | MET108 |
| F | GLY109 |
| F | SER111 |
| F | GLY141 |
| F | ALA143 |
| F | HOH6104 |
| F | HOH6416 |
| F | HOH6442 |
| F | HOH6537 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MPD F 6006 |
| Chain | Residue |
| F | LYS251 |
| F | ASN268 |
| F | TRP303 |
| F | ASP305 |
| F | HOH6246 |
| F | HOH6270 |
| F | HOH6284 |
| F | HOH6546 |
| F | HOH6563 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| A | SER415 | |
| A | GLY414 | |
| D | GLY181 | |
| D | GLY182 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| E | GLY181 | |
| E | GLY182 | |
| B | SER415 | |
| B | GLY414 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| F | GLY181 | |
| F | GLY182 | |
| C | SER415 | |
| C | GLY414 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| A | GLY181 | |
| A | GLY182 | |
| D | SER415 | |
| D | GLY414 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| E | SER415 | |
| E | GLY414 | |
| B | GLY181 | |
| B | GLY182 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| F | SER415 | |
| F | GLY414 | |
| C | GLY181 | |
| C | GLY182 |
