1VRG
Crystal structure of propionyl-CoA carboxylase, beta subunit (TM0716) from THERMOTOGA MARITIMA at 2.30 A resolution
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 | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| A | 0015977 | biological_process | carbon fixation |
| A | 0016874 | molecular_function | ligase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| B | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| B | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| B | 0015977 | biological_process | carbon fixation |
| B | 0016874 | molecular_function | ligase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| C | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| C | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| C | 0015977 | biological_process | carbon fixation |
| C | 0016874 | molecular_function | ligase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| D | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| D | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| D | 0015977 | biological_process | carbon fixation |
| D | 0016874 | molecular_function | ligase activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| E | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| E | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| E | 0015977 | biological_process | carbon fixation |
| E | 0016874 | molecular_function | ligase activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| F | 0004658 | molecular_function | propionyl-CoA carboxylase activity |
| F | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| F | 0015977 | biological_process | carbon fixation |
| F | 0016874 | molecular_function | ligase activity |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 516 |
| Chain | Residue |
| C | HIS379 |
| C | HOH598 |
| C | HOH699 |
| F | HIS379 |
| F | HOH656 |
| F | HOH679 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 516 |
| Chain | Residue |
| B | HOH749 |
| E | HIS379 |
| E | HOH774 |
| B | HIS379 |
| B | HOH620 |
| B | HOH652 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 516 |
| Chain | Residue |
| A | HIS379 |
| D | HIS379 |
| D | HOH665 |
| D | HOH712 |
| D | HOH739 |
| D | HOH744 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BCT E 516 |
| Chain | Residue |
| E | GLY196 |
| E | PRO197 |
| E | ASN198 |
| E | VAL199 |
| E | HOH709 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BCT A 517 |
| Chain | Residue |
| A | GLY196 |
| A | PRO197 |
| A | ASN198 |
| A | VAL199 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BCT B 517 |
| Chain | Residue |
| B | GLY196 |
| B | PRO197 |
| B | ASN198 |
| B | VAL199 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BCT C 517 |
| Chain | Residue |
| C | GLY196 |
| C | PRO197 |
| C | ASN198 |
| C | VAL199 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BCT D 516 |
| Chain | Residue |
| D | GLY196 |
| D | PRO197 |
| D | ASN198 |
| D | VAL199 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BCT F 516 |
| Chain | Residue |
| F | GLY196 |
| F | PRO197 |
| F | ASN198 |
| F | VAL199 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BCT B 518 |
| Chain | Residue |
| B | PRO275 |
| B | ASP276 |
| B | ASN277 |
| B | LYS280 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BCT C 518 |
| Chain | Residue |
| C | PRO275 |
| C | ASP276 |
| C | ASN277 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BCT D 517 |
| Chain | Residue |
| D | LEU118 |
| D | LYS119 |
| D | GLY121 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BCT E 517 |
| Chain | Residue |
| E | PRO275 |
| E | ASP276 |
| E | ASN277 |
| E | LYS280 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| A | ALA406 | |
| A | GLY405 | |
| D | GLY172 | |
| D | GLY171 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| E | GLY172 | |
| E | GLY171 | |
| B | ALA406 | |
| B | GLY405 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| F | GLY172 | |
| F | GLY171 | |
| C | ALA406 | |
| C | GLY405 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| A | GLY172 | |
| A | GLY171 | |
| D | ALA406 | |
| D | GLY405 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| E | ALA406 | |
| E | GLY405 | |
| B | GLY172 | |
| B | GLY171 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| F | ALA406 | |
| F | GLY405 | |
| C | GLY172 | |
| C | GLY171 |
