2R9E
The structure of the binary complex of citryl dethia COA and citrate synthase from the thermophilic archaeonthermoplasma acidophilum
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004108 | molecular_function | citrate (Si)-synthase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
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 | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
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 | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
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 | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
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 | 29 |
Details | BINDING SITE FOR RESIDUE SDX A 700 |
Chain | Residue |
A | HIS187 |
A | PHE260 |
A | GLY261 |
A | HIS262 |
A | ARG263 |
A | ARG271 |
A | ILE312 |
A | ASN315 |
A | ASP317 |
A | ARG344 |
A | HOH1056 |
A | PRO190 |
A | HOH1595 |
A | HOH1606 |
A | HOH1750 |
A | HOH2269 |
A | HOH2323 |
A | HOH2324 |
A | HOH2325 |
A | HOH2326 |
B | ARG361 |
B | ARG364 |
A | LEU221 |
A | HIS222 |
A | ALA225 |
A | ARG256 |
A | LEU257 |
A | MET258 |
A | GLY259 |
site_id | AC2 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE SDX B 701 |
Chain | Residue |
A | ARG361 |
A | ARG364 |
A | HOH2322 |
B | HIS187 |
B | PRO190 |
B | LEU221 |
B | HIS222 |
B | ALA225 |
B | ARG256 |
B | LEU257 |
B | GLY259 |
B | PHE260 |
B | GLY261 |
B | HIS262 |
B | ARG263 |
B | ARG271 |
B | ILE312 |
B | ASN315 |
B | ARG344 |
B | HOH1052 |
B | HOH1150 |
B | HOH1459 |
B | HOH1483 |
B | HOH1611 |
B | HOH2036 |
B | HOH2059 |
B | HOH2265 |
B | HOH2319 |
B | HOH2320 |
B | HOH2321 |
site_id | AC3 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE SDX C 702 |
Chain | Residue |
C | HIS187 |
C | PRO190 |
C | LEU221 |
C | HIS222 |
C | ALA225 |
C | ARG256 |
C | LEU257 |
C | GLY259 |
C | PHE260 |
C | GLY261 |
C | HIS262 |
C | ARG263 |
C | ARG271 |
C | ILE312 |
C | ASN315 |
C | ASP317 |
C | ARG344 |
C | HOH1040 |
C | HOH1074 |
C | HOH1098 |
C | HOH1214 |
C | HOH2294 |
C | HOH2317 |
C | HOH2318 |
D | ARG361 |
D | ARG364 |
site_id | AC4 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE SDX D 703 |
Chain | Residue |
D | HIS262 |
D | ARG263 |
D | ARG271 |
D | LYS310 |
D | ILE312 |
D | ASN315 |
D | ASP317 |
D | ARG344 |
D | HOH1054 |
D | HOH1133 |
D | HOH1598 |
D | HOH2327 |
D | HOH2328 |
D | HOH2329 |
D | HOH2330 |
B | GLU148 |
B | LYS151 |
C | ARG361 |
C | ARG364 |
D | HIS187 |
D | PRO190 |
D | LEU221 |
D | HIS222 |
D | ALA225 |
D | ARG256 |
D | LEU257 |
D | GLY259 |
D | PHE260 |
D | GLY261 |
Functional Information from PROSITE/UniProt
site_id | PS00480 |
Number of Residues | 13 |
Details | CITRATE_SYNTHASE Citrate synthase signature. GFGHrVy.KtyDPR |
Chain | Residue | Details |
A | GLY259-ARG271 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:7704526 |
Chain | Residue | Details |
A | HIS222 | |
D | HIS222 | |
D | HIS262 | |
D | ASP317 | |
A | HIS262 | |
A | ASP317 | |
B | HIS222 | |
B | HIS262 | |
B | ASP317 | |
C | HIS222 | |
C | HIS262 | |
C | ASP317 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1aj8 |
Chain | Residue | Details |
A | ASP317 | |
A | HIS262 | |
A | HIS222 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1aj8 |
Chain | Residue | Details |
B | ASP317 | |
B | HIS262 | |
B | HIS222 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1aj8 |
Chain | Residue | Details |
C | ASP317 | |
C | HIS262 | |
C | HIS222 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1aj8 |
Chain | Residue | Details |
D | ASP317 | |
D | HIS262 | |
D | HIS222 |
site_id | CSA5 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1aj8 |
Chain | Residue | Details |
A | SER192 | |
A | HIS262 | |
A | ASP317 | |
A | HIS222 |
site_id | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1aj8 |
Chain | Residue | Details |
B | SER192 | |
B | HIS262 | |
B | ASP317 | |
B | HIS222 |
site_id | CSA7 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1aj8 |
Chain | Residue | Details |
C | SER192 | |
C | HIS262 | |
C | ASP317 | |
C | HIS222 |
site_id | CSA8 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1aj8 |
Chain | Residue | Details |
D | SER192 | |
D | HIS262 | |
D | ASP317 | |
D | HIS222 |