Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004108 | molecular_function | citrate (Si)-synthase activity |
A | 0006099 | biological_process | tricarboxylic acid cycle |
A | 0006101 | biological_process | citrate metabolic process |
A | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
B | 0004108 | molecular_function | citrate (Si)-synthase activity |
B | 0006099 | biological_process | tricarboxylic acid cycle |
B | 0006101 | biological_process | citrate metabolic process |
B | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE COF A 700 |
Chain | Residue |
A | HIS274 |
A | ALA277 |
A | GLU280 |
A | TRP284 |
A | ARG313 |
A | VAL314 |
A | VAL315 |
A | PRO316 |
A | GLY317 |
A | TYR318 |
A | GLY319 |
A | HIS320 |
A | ALA321 |
A | LYS366 |
A | ALA367 |
A | LYS368 |
A | ASN373 |
A | ASP375 |
A | CIT701 |
A | HOH703 |
A | HOH727 |
A | HOH734 |
A | HOH751 |
A | HOH764 |
B | TYR158 |
B | ARG164 |
B | LEU419 |
A | ARG46 |
A | PRO272 |
A | LEU273 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE CIT A 701 |
Chain | Residue |
A | HIS238 |
A | ASN242 |
A | HIS274 |
A | HIS320 |
A | ARG329 |
A | ASP375 |
A | ARG401 |
A | COF700 |
A | HOH751 |
B | ARG421 |
site_id | AC3 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE COF B 700 |
Chain | Residue |
A | TYR158 |
A | ARG164 |
A | LEU419 |
B | ARG46 |
B | PRO272 |
B | LEU273 |
B | HIS274 |
B | ALA277 |
B | ARG313 |
B | VAL314 |
B | VAL315 |
B | PRO316 |
B | GLY317 |
B | TYR318 |
B | GLY319 |
B | HIS320 |
B | ALA321 |
B | LYS366 |
B | ALA367 |
B | LYS368 |
B | ASN373 |
B | ASP375 |
B | CIT701 |
B | HOH738 |
B | HOH745 |
B | HOH773 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE CIT B 701 |
Chain | Residue |
A | ARG421 |
B | HIS238 |
B | ASN242 |
B | HIS274 |
B | HIS320 |
B | ARG329 |
B | ASP375 |
B | ARG401 |
B | COF700 |
B | HOH762 |
site_id | ACA |
Number of Residues | 3 |
Details | ENZYME ACTIVE SITE. |
Chain | Residue |
A | HIS274 |
A | HIS320 |
A | ASP375 |
site_id | ACB |
Number of Residues | 3 |
Details | ENZYME ACTIVE SITE. |
Chain | Residue |
B | HIS274 |
B | HIS320 |
B | ASP375 |
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 | 6 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | HIS274 | |
A | HIS320 | |
A | ASP375 | |
B | HIS274 | |
B | HIS320 | |
B | ASP375 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 78 |
Chain | Residue | Details |
A | SER244 | electrostatic stabiliser, hydrogen bond donor |
A | HIS274 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
A | HIS320 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
A | ARG329 | electrostatic stabiliser |
A | ASP375 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 78 |
Chain | Residue | Details |
B | SER244 | electrostatic stabiliser, hydrogen bond donor |
B | HIS274 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
B | HIS320 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
B | ARG329 | electrostatic stabiliser |
B | ASP375 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |