2C6X
Structure of Bacillus subtilis citrate synthase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004108 | molecular_function | citrate (Si)-synthase activity |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0016740 | molecular_function | transferase activity |
| A | 0036440 | molecular_function | citrate synthase activity |
| A | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
| B | 0004108 | molecular_function | citrate (Si)-synthase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0016740 | molecular_function | transferase activity |
| B | 0036440 | molecular_function | citrate synthase activity |
| B | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
| C | 0004108 | molecular_function | citrate (Si)-synthase activity |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0016740 | molecular_function | transferase activity |
| C | 0036440 | molecular_function | citrate synthase activity |
| C | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
| D | 0004108 | molecular_function | citrate (Si)-synthase activity |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0006099 | biological_process | tricarboxylic acid cycle |
| D | 0016740 | molecular_function | transferase activity |
| D | 0036440 | molecular_function | citrate synthase activity |
| D | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE COZ A1365 |
| Chain | Residue |
| A | GLN144 |
| A | LYS297 |
| A | ARG300 |
| A | LEU302 |
| A | ASN305 |
| A | GLU307 |
| A | ALA219 |
| A | ARG246 |
| A | LEU247 |
| A | MET248 |
| A | PHE250 |
| A | GLY251 |
| A | HIS252 |
| A | ARG253 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CIT A1366 |
| Chain | Residue |
| A | HIS178 |
| A | ASN181 |
| A | HIS213 |
| A | GLY214 |
| A | ARG261 |
| A | GLU307 |
| A | ARG332 |
| B | ARG351 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE COZ B1365 |
| Chain | Residue |
| B | ALA219 |
| B | ARG246 |
| B | LEU247 |
| B | MET248 |
| B | PHE250 |
| B | GLY251 |
| B | HIS252 |
| B | ARG253 |
| B | LYS297 |
| B | ARG300 |
| B | LEU302 |
| B | ASN305 |
| B | GLU307 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CIT B1366 |
| Chain | Residue |
| A | ARG351 |
| B | HIS178 |
| B | ASN181 |
| B | HIS213 |
| B | GLY214 |
| B | ARG261 |
| B | GLU307 |
| B | ARG332 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE COZ C1365 |
| Chain | Residue |
| C | GLN144 |
| C | ALA219 |
| C | ARG246 |
| C | LEU247 |
| C | MET248 |
| C | PHE250 |
| C | GLY251 |
| C | HIS252 |
| C | ARG253 |
| C | LYS297 |
| C | ARG300 |
| C | LEU302 |
| C | ASN305 |
| C | GLU307 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CIT C1366 |
| Chain | Residue |
| C | HIS178 |
| C | ASN181 |
| C | HIS213 |
| C | GLY214 |
| C | ARG261 |
| C | GLU307 |
| C | ARG332 |
| D | ARG351 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE COZ D1365 |
| Chain | Residue |
| D | ALA219 |
| D | ARG246 |
| D | LEU247 |
| D | MET248 |
| D | PHE250 |
| D | GLY251 |
| D | HIS252 |
| D | ARG253 |
| D | LYS297 |
| D | ARG300 |
| D | LEU302 |
| D | ASN305 |
| D | GLU307 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CIT D1366 |
| Chain | Residue |
| C | ARG351 |
| D | HIS178 |
| D | ASN181 |
| D | HIS213 |
| D | GLY214 |
| D | ARG261 |
| D | GLU307 |
| D | ARG332 |
Functional Information from PROSITE/UniProt
| site_id | PS00480 |
| Number of Residues | 13 |
| Details | CITRATE_SYNTHASE Citrate synthase signature. GFGHrVy.KtkDPR |
| Chain | Residue | Details |
| A | GLY249-ARG261 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10117 |
| Chain | Residue | Details |
| A | HIS252 | |
| A | GLU307 | |
| B | HIS252 | |
| B | GLU307 | |
| C | HIS252 | |
| C | GLU307 | |
| D | HIS252 | |
| D | GLU307 |
