5CSC
STRUCTURE OF AN OPEN FORM OF CHICKEN HEART CITRATE SYNTHASE AT 2.8 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004108 | molecular_function | citrate (Si)-synthase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006101 | biological_process | citrate metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0036440 | molecular_function | citrate synthase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
| B | 0004108 | molecular_function | citrate (Si)-synthase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006101 | biological_process | citrate metabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0036440 | molecular_function | citrate synthase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
Functional Information from PROSITE/UniProt
| site_id | PS00480 |
| Number of Residues | 13 |
| Details | CITRATE_SYNTHASE Citrate synthase signature. GYGHaVl.RktDPR |
| Chain | Residue | Details |
| A | GLY317-ARG329 | |
| B | GLY317-ARG329 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| B | GLY275 | |
| B | ARG324 | |
| B | GLY379 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1aj8 |
| Chain | Residue | Details |
| A | ASP375 | |
| A | HIS274 | |
| A | HIS320 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1aj8 |
| Chain | Residue | Details |
| B | ASP375 | |
| B | HIS274 | |
| B | HIS320 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1aj8 |
| Chain | Residue | Details |
| A | ASP375 | |
| A | HIS320 | |
| A | HIS274 | |
| A | SER244 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1aj8 |
| Chain | Residue | Details |
| B | ASP375 | |
| B | HIS320 | |
| B | HIS274 | |
| B | SER244 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 78 |
| Chain | Residue | Details |
| B | ALA245 | electrostatic stabiliser, hydrogen bond donor |
| B | GLY275 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | ARG324 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | GLN333 | electrostatic stabiliser |
| B | GLY379 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
