eF-site ID 1cts-A PDB Code 1cts Chain A click to enlarge Title CRYSTALLOGRAPHIC REFINEMENT AND ATOMIC MODELS OF TWO DIFFERENT FORMS OF CITRATE SYNTHASE AT 2.7 AND 1.7 ANGSTROMS RESOLUTION Classification OXO-ACID-LYASE Compound CITRATE SYNTHASE Source Sus scrofa (Pig) (CISY_PIG) Sequence A:  ASSTNLKDILADLIPKEQARIKTFRQQHGNTVVGQITVDM MYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPK AKGGEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAAL PSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAE GIHRTKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSI GAIDSKLDWSHNFTNMLGYTDAQFTELMRLYLTIHSDHEG GNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQE VLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGH AVLRKTDPRYTCQREFALKHLPHDPMFKLVAQLYKIVPNV LLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVS RALGVLAQLIWSRALGFPLERPKSMSTDGLIKLVDSK Description Functional site 1) chain A residue 238 type sequence H description BINDING SITE FOR RESIDUE CIT A 438 source : AC1 2) chain A residue 242 type sequence N description BINDING SITE FOR RESIDUE CIT A 438 source : AC1 3) chain A residue 274 type sequence H description BINDING SITE FOR RESIDUE CIT A 438 source : AC1 4) chain A residue 401 type sequence R description BINDING SITE FOR RESIDUE CIT A 438 source : AC1 5) chain A residue 317-329 type prosite sequence GYGHAVLRKTDPR description CITRATE_SYNTHASE Citrate synthase signature. GYGHaVl.RktDPR source prosite : PS00480 6) chain A residue 274 type ACT_SITE sequence H description source Swiss-Prot : SWS_FT_FI1 7) chain A residue 320 type ACT_SITE sequence H description source Swiss-Prot : SWS_FT_FI1 8) chain A residue 375 type ACT_SITE sequence D description source Swiss-Prot : SWS_FT_FI1 9) chain A residue 49 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q29RK1 source Swiss-Prot : SWS_FT_FI2 10) chain A residue 76 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CZU6 source Swiss-Prot : SWS_FT_FI3 11) chain A residue 166 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CZU6 source Swiss-Prot : SWS_FT_FI3 12) chain A residue 423 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CZU6 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 199 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9CZU6 source Swiss-Prot : SWS_FT_FI4 14) chain A residue 294 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CZU6 source Swiss-Prot : SWS_FT_FI5 15) chain A residue 300 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CZU6 source Swiss-Prot : SWS_FT_FI5 16) chain A residue 348 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CZU6 source Swiss-Prot : SWS_FT_FI5 17) chain A residue 366 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CZU6 source Swiss-Prot : SWS_FT_FI5 18) chain A residue 432 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CZU6 source Swiss-Prot : SWS_FT_FI5 19) chain A residue 355 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O75390 source Swiss-Prot : SWS_FT_FI6 20) chain A residue 368 type MOD_RES sequence K description N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:7093227 source Swiss-Prot : SWS_FT_FI7

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