Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004108 | molecular_function | obsolete 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ACO A 700 |
| Chain | Residue |
| A | ARG46 |
| A | TYR318 |
| A | GLY319 |
| A | HIS320 |
| A | ALA321 |
| A | ALA366 |
| A | ALA367 |
| A | ALA368 |
| A | ASN373 |
| A | ASP375 |
| A | PHE397 |
| A | ARG164 |
| A | HOH539 |
| A | HOH547 |
| A | HOH585 |
| A | HOH603 |
| A | MLT702 |
| A | LEU273 |
| A | HIS274 |
| A | ALA277 |
| A | LEU309 |
| A | VAL314 |
| A | VAL315 |
| A | GLY317 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MLT A 702 |
| Chain | Residue |
| A | HIS238 |
| A | ASN242 |
| A | HIS274 |
| A | HIS320 |
| A | ARG329 |
| A | ARG401 |
| A | ARG421 |
| A | HOH584 |
| A | HOH586 |
| A | ACO700 |
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 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"in chain A","evidences":[{"source":"UniProtKB","id":"O75390","evidenceCode":"ECO:0000250"}]} |
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 | 4 |
| Details | Annotated By Reference To The Literature 1aj8 |
| Chain | Residue | Details |
| A | ASP375 | |
| A | HIS320 | |
| A | HIS274 | |
| A | SER244 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 78 |
| Chain | Residue | Details |
| A | SER248 | electrostatic stabiliser, hydrogen bond donor |
| A | ASN278 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | PHE336 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | PRO345 | electrostatic stabiliser |
| A | ASN391 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
