1OWC
Three Dimensional Structure Analysis Of The R109L Variant of the Type II Citrate Synthase From E. Coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004108 | molecular_function | citrate (Si)-synthase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0034214 | biological_process | protein hexamerization |
| 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 |
| A | 0070404 | molecular_function | NADH binding |
| B | 0004108 | molecular_function | citrate (Si)-synthase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0034214 | biological_process | protein hexamerization |
| 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 |
| B | 0070404 | molecular_function | NADH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2001 |
| Chain | Residue |
| A | ARG407 |
| B | HOH16 |
| B | HOH397 |
| B | ASN1232 |
| B | ALA1233 |
| B | ARG1299 |
| B | ARG1306 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2002 |
| Chain | Residue |
| A | HOH2065 |
| B | LYS1055 |
| A | GLY414 |
| A | TYR415 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2003 |
| Chain | Residue |
| B | HOH16 |
| B | HOH73 |
| B | HIS1229 |
| B | ASN1232 |
| B | ARG1299 |
| B | HIS1305 |
| B | ARG1314 |
| B | ARG1387 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2004 |
| Chain | Residue |
| A | ASN232 |
| A | ALA233 |
| A | ARG299 |
| A | ARG306 |
| A | HOH2034 |
| A | HOH2111 |
| B | ILE1405 |
| B | ARG1407 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2005 |
| Chain | Residue |
| A | LYS55 |
| B | HOH86 |
| B | THR1413 |
| B | GLY1414 |
| B | TYR1415 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2006 |
| Chain | Residue |
| A | HIS229 |
| A | ASN232 |
| A | ARG299 |
| A | HIS305 |
| A | ARG314 |
| A | ARG387 |
| A | HOH2015 |
| A | HOH2111 |
| A | HOH2112 |
Functional Information from PROSITE/UniProt
| site_id | PS00480 |
| Number of Residues | 13 |
| Details | CITRATE_SYNTHASE Citrate synthase signature. GFGHrVy.KnyDPR |
| Chain | Residue | Details |
| A | GLY302-ARG314 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10117 |
| Chain | Residue | Details |
| A | HIS305 | |
| A | ASP362 | |
| B | HIS1305 | |
| B | ASP1362 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS282 | |
| B | LYS1282 |
