1PIX
Crystal structure of the carboxyltransferase subunit of the bacterial ion pump glutaconyl-coenzyme A decarboxylase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004485 | molecular_function | methylcrotonoyl-CoA carboxylase activity |
| A | 0006552 | biological_process | L-leucine catabolic process |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0006814 | biological_process | sodium ion transport |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0016874 | molecular_function | ligase activity |
| A | 0018801 | molecular_function | glutaconyl-CoA decarboxylase activity |
| A | 0019552 | biological_process | L-glutamate catabolic process via 2-hydroxyglutarate |
| A | 0055085 | biological_process | transmembrane transport |
| A | 1905202 | cellular_component | methylcrotonoyl-CoA carboxylase complex |
| B | 0004485 | molecular_function | methylcrotonoyl-CoA carboxylase activity |
| B | 0006552 | biological_process | L-leucine catabolic process |
| B | 0006811 | biological_process | monoatomic ion transport |
| B | 0006814 | biological_process | sodium ion transport |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0016874 | molecular_function | ligase activity |
| B | 0018801 | molecular_function | glutaconyl-CoA decarboxylase activity |
| B | 0019552 | biological_process | L-glutamate catabolic process via 2-hydroxyglutarate |
| B | 0055085 | biological_process | transmembrane transport |
| B | 1905202 | cellular_component | methylcrotonoyl-CoA carboxylase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2000 |
| Chain | Residue |
| A | ARG164 |
| B | HOH1435 |
| B | HOH1573 |
| A | ARG172 |
| A | HOH1009 |
| A | HOH1306 |
| B | ARG164 |
| B | ARG172 |
| B | HOH1110 |
| B | HOH1260 |
| B | HOH1305 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2001 |
| Chain | Residue |
| A | TYR268 |
| A | ALA269 |
| A | SER270 |
| A | GLY273 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2002 |
| Chain | Residue |
| A | GLU46 |
| A | ALA50 |
| A | ASP51 |
| A | LYS114 |
| A | HOH1643 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2003 |
| Chain | Residue |
| B | GLU46 |
| B | ALA50 |
| B | ASP51 |
| B | LYS114 |
| B | HOH1096 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2004 |
| Chain | Residue |
| B | TYR268 |
| B | ALA269 |
| B | SER270 |
| B | GLY273 |
| B | HOH1075 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT B 2005 |
| Chain | Residue |
| B | THR137 |
| B | HIS443 |
| B | ILE444 |
| B | PRO445 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 2006 |
| Chain | Residue |
| A | THR137 |
| A | ILE444 |
| A | PRO445 |
| A | ASP469 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 2007 |
| Chain | Residue |
| A | ARG7 |
| A | TYR8 |
| A | HIS336 |
| A | ARG578 |
| A | HOH1480 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 2008 |
| Chain | Residue |
| A | ALA300 |
| A | ASN354 |
| A | ARG548 |
| A | GLU552 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 534 |
| Details | Domain: {"description":"CoA carboxyltransferase N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU01136","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 526 |
| Details | Domain: {"description":"CoA carboxyltransferase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU01137","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1054 |
| Details | Region: {"description":"Carboxyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01138","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 12853465 |
| Chain | Residue | Details |
| A | ILE417 | |
| A | VAL151 | |
| A | ALA457 | |
| A | GLY194 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 12853465 |
| Chain | Residue | Details |
| B | ILE417 | |
| B | VAL151 | |
| B | ALA457 | |
| B | GLY194 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 675 |
| Chain | Residue | Details |
| A | VAL151 | electrostatic stabiliser |
| A | GLY194 | electrostatic stabiliser |
| A | ILE417 | electrostatic stabiliser |
| A | ALA457 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 675 |
| Chain | Residue | Details |
| B | VAL151 | electrostatic stabiliser |
| B | GLY194 | electrostatic stabiliser |
| B | ILE417 | electrostatic stabiliser |
| B | ALA457 | electrostatic stabiliser |
