eF-site ID 1a3w-A PDB Code 1a3w Chain A click to enlarge Title PYRUVATE KINASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH FBP, PG, MN2+ AND K+ Classification TRANSFERASE Compound PYRUVATE KINASE Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence A:  SRLERLTSLSDLRRTSIIGTIGPKTNNPETLVALRKAGLN IVRMNFSHGSYEYHKSVIDNARKSEELYPGRPLAIALDTK GPEIRTGTTTNDVDYPIPPNHEMIFTTDDKYAKACDDKIM YVDYKNITKVISAGRIIYVDDGVLSFQVLEVVDTLKVKAL NAGKICSHKGVNLPGTDVDLPALSEKDKEDLRFGVKNGVH MVFASFIRTANDVLTIREVLGEQGKDVKIIVKIENQQGVN NFDEILKVTDGVMVARGDLGIEIPAPEVLAVQKKLIAKSN LAGKPVICATQMLESMTYNPRPTRAEVSDVGNAILDGADC VMLSGETAKGNYPINAVTTMAETAVIAEQAIAYLPNYDDM RNCTPKPTSTTETVAASAVAAVFEQKAKAIIVLSTSGTTP RLVSKYRPNCPIILVTRCPRAARFSHLYRGVFPFVFEKEP VSDWTDDVEARINFGIEKAKEFGILKKGDTYVSIQGFKAG AGHSNTLQVSTV Description Functional site 1) chain A residue 49 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9519410, ECO:0007744|PDB:1A3X source Swiss-Prot : SWS_FT_FI1 2) chain A residue 240 type BINDING sequence K description BINDING => ECO:0000269|PubMed:9519410, ECO:0007744|PDB:1A3X source Swiss-Prot : SWS_FT_FI1 3) chain A residue 70 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI10 4) chain A residue 316 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI10 5) chain A residue 450 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI10 6) chain A residue 213 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17287358 source Swiss-Prot : SWS_FT_FI11 7) chain A residue 478 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI12 8) chain A residue 91 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 9) chain A residue 177 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 10) chain A residue 235-247 type prosite sequence VKIIVKIENQQGV description PYRUVATE_KINASE Pyruvate kinase active site signature. VkIIVKIENqQGV source prosite : PS00110 11) chain A residue 204 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI13 12) chain A residue 255 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI13 13) chain A residue 446 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI13 14) chain A residue 51 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9519410, ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X source Swiss-Prot : SWS_FT_FI2 15) chain A residue 484 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9519410, ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X source Swiss-Prot : SWS_FT_FI2 16) chain A residue 53 type BINDING sequence S description BINDING => ECO:0000269|PubMed:9519410, ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X source Swiss-Prot : SWS_FT_FI2 17) chain A residue 84 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9519410, ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X source Swiss-Prot : SWS_FT_FI2 18) chain A residue 85 type BINDING sequence T description BINDING => ECO:0000269|PubMed:9519410, ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X source Swiss-Prot : SWS_FT_FI2 19) chain A residue 242 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9519410, ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X source Swiss-Prot : SWS_FT_FI2 20) chain A residue 265 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9519410, ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X source Swiss-Prot : SWS_FT_FI2 21) chain A residue 298 type BINDING sequence T description BINDING => ECO:0000269|PubMed:9519410, ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X source Swiss-Prot : SWS_FT_FI2 22) chain A residue 452 type BINDING sequence W description BINDING => ECO:0000269|PubMed:9519410, ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X source Swiss-Prot : SWS_FT_FI2 23) chain A residue 459 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9519410, ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X source Swiss-Prot : SWS_FT_FI2 24) chain A residue 266 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9519410, ECO:0007744|PDB:1A3W source Swiss-Prot : SWS_FT_FI4 25) chain A residue 402 type BINDING sequence S description BINDING => ECO:0000269|PubMed:9519410, ECO:0007744|PDB:1A3W source Swiss-Prot : SWS_FT_FI4 26) chain A residue 240 type SITE sequence K description Transition state stabilizer => ECO:0000269|PubMed:10413488 source Swiss-Prot : SWS_FT_FI5 27) chain A residue 2 type MOD_RES sequence S description N-acetylserine => ECO:0007744|PubMed:17287358 source Swiss-Prot : SWS_FT_FI6 28) chain A residue 9 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI7 29) chain A residue 16 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI8 30) chain A residue 31 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI9 31) chain A residue 184 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI9

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