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 | 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 | 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 | 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 | 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 | GLU282 | |
B | GLU1282 |