4JAE
STRUCTURAL DETERMINATION OF THE A50T:S279G:S280K:V281K:K282E:H283N VARIANT OF CITRATE SYNTHASE FROM E. COLI complexed WITH S-CARBOXYMETHYL-COA
Replaces: 3L97Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004108 | molecular_function | obsolete 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 | 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 | 0003824 | molecular_function | catalytic activity |
| B | 0004108 | molecular_function | obsolete 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 | 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 | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 501 |
| Chain | Residue |
| A | HIS229 |
| A | ASN232 |
| A | ARG299 |
| A | HIS305 |
| A | ARG314 |
| A | ARG387 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 502 |
| Chain | Residue |
| B | TYR1415 |
| A | LYS55 |
| B | THR1413 |
| B | GLY1414 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CMC A 503 |
| Chain | Residue |
| A | THR106 |
| A | THR108 |
| A | ARG109 |
| A | HIS110 |
| A | THR111 |
| A | MET112 |
| A | GLU158 |
| A | ILE159 |
| A | PHE162 |
| A | ARG163 |
| A | LYS167 |
| A | GLN182 |
| A | ASN189 |
| A | CYS206 |
| A | HOH666 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2001 |
| Chain | Residue |
| A | GLY414 |
| B | LYS1055 |
| B | HOH2118 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2002 |
| Chain | Residue |
| B | HIS1229 |
| B | ASN1232 |
| B | HIS1305 |
| B | ARG1387 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CMC B 2003 |
| Chain | Residue |
| B | THR1105 |
| B | THR1106 |
| B | THR1108 |
| B | ARG1109 |
| B | HIS1110 |
| B | THR1111 |
| B | MET1112 |
| B | TYR1145 |
| B | ILE1159 |
| B | PHE1162 |
| B | ARG1163 |
| B | LYS1167 |
| B | ASN1189 |
| B | CYS1206 |
| B | HOH2133 |
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 | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10117","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
