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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE OAA A 702 |
| Chain | Residue |
| A | HIS238 |
| A | ASN242 |
| A | HIS274 |
| A | HIS320 |
| A | ARG329 |
| A | ARG401 |
| A | ARG421 |
| A | HOH584 |
| A | FCX700 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FCX A 700 |
| Chain | Residue |
| A | ARG46 |
| A | ARG164 |
| A | LEU273 |
| A | HIS274 |
| A | ALA277 |
| A | LEU309 |
| A | VAL314 |
| A | VAL315 |
| A | GLY317 |
| A | TYR318 |
| A | GLY319 |
| A | HIS320 |
| A | ALA321 |
| A | LYS366 |
| A | ALA367 |
| A | LYS368 |
| A | ASN373 |
| A | ASP375 |
| A | HOH539 |
| A | HOH547 |
| A | HOH585 |
| A | HOH603 |
| A | HOH623 |
| A | OAA702 |
| site_id | FCX |
| Number of Residues | 8 |
| Details | |
| Chain | Residue |
| A | ARG46 |
| A | HIS274 |
| A | VAL315 |
| A | GLY317 |
| A | TYR318 |
| A | LYS366 |
| A | LYS368 |
| A | ASP375 |
| site_id | OAA |
| Number of Residues | 4 |
| Details | |
| Chain | Residue |
| A | HIS320 |
| A | ARG329 |
| A | ARG401 |
| A | HIS238 |
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 | ACT_SITE: |
| Chain | Residue | Details |
| A | THR247 | |
| A | GLY293 | |
| A | LYS348 | |
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 | LEU217 | electrostatic stabiliser, hydrogen bond donor |
| A | THR247 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | GLY293 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | ARG302 | electrostatic stabiliser |
| A | LYS348 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
