eF-site ID 1a3x-B PDB Code 1a3x Chain B click to enlarge Title PYRUVATE KINASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH PG, MN2+ AND K+ Classification TRANSFERASE Compound PYRUVATE KINASE Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence B:  MSRLERLTSLNVVAGSDLRRTSIIGTIGPKTNNPETLVAL RKAGLNIVRMNFSHGSYEYHKSVIDNARKSEELYPGRPLA IALDTKGPEIRTGTTTNDVDYPIPPNHEMIFTTDDKYAKA CDDKIMYVDYKNITKVISAGRIIYVDDGVLSFQVLEVVDD KTLKVKALNAGKICSHKGVNLPGTDVDLPALSEKDKEDLR FGVKNGVHMVFASFIRTANDVLTIREVLGEQGKDVKIIVK IENQQGVNNFDEILKVTDGVMVARGDLGIEIPAPEVLAVQ KKLIAKSNLAGKPVICATQMLESMTYNPRPTRAEVSDVGN AILDGADCVMLSGETAKGNYPINAVTTMAETAVIAEQAIA YLPNYDDMRNCTPKPTSTTETVAASAVAAVFEQKAKAIIV LSTSGTTPRLVSKYRPNCPIILVTRCPRAARFSHLYRGVF PFVFEKETDDVEARINFGIEKAKEFGILKKGDTYVSIQGN TLQVSTV Description Functional site 1) chain B residue 49 type sequence R description BINDING SITE FOR RESIDUE PGA B 1006 source : AC2 2) chain B residue 213 type sequence S description BINDING SITE FOR RESIDUE PGA B 1006 source : AC2 3) chain B residue 240 type sequence K description BINDING SITE FOR RESIDUE PGA B 1006 source : AC2 4) chain B residue 242 type sequence E description BINDING SITE FOR RESIDUE PGA B 1006 source : AC2 5) chain B residue 263 type sequence A description BINDING SITE FOR RESIDUE PGA B 1006 source : AC2 6) chain B residue 264 type sequence R description BINDING SITE FOR RESIDUE PGA B 1006 source : AC2 7) chain B residue 265 type sequence G description BINDING SITE FOR RESIDUE PGA B 1006 source : AC2 8) chain B residue 266 type sequence D description BINDING SITE FOR RESIDUE PGA B 1006 source : AC2 9) chain B residue 297 type sequence A description BINDING SITE FOR RESIDUE PGA B 1006 source : AC2 10) chain B residue 298 type sequence T description BINDING SITE FOR RESIDUE PGA B 1006 source : AC2 11) chain B residue 242 type sequence E description BINDING SITE FOR RESIDUE MN B 1003 source : AC5 12) chain B residue 266 type sequence D description BINDING SITE FOR RESIDUE MN B 1003 source : AC5 13) chain B residue 51 type sequence N description BINDING SITE FOR RESIDUE K B 1004 source : AC6 14) chain B residue 53 type sequence S description BINDING SITE FOR RESIDUE K B 1004 source : AC6 15) chain B residue 84 type sequence D description BINDING SITE FOR RESIDUE K B 1004 source : AC6 16) chain B residue 85 type sequence T description BINDING SITE FOR RESIDUE K B 1004 source : AC6 17) chain B residue 213 type sequence S description BINDING SITE FOR RESIDUE K B 1004 source : AC6 18) chain B residue 49 type BINDING sequence R description BINDING => ECO:0000269|PubMed:9519410, ECO:0007744|PDB:1A3X source Swiss-Prot : SWS_FT_FI1 19) chain B residue 240 type BINDING sequence K description BINDING => ECO:0000269|PubMed:9519410, ECO:0007744|PDB:1A3X source Swiss-Prot : SWS_FT_FI1 20) chain B residue 91 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 21) chain B residue 177 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 266 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9519410, ECO:0007744|PDB:1A3W source Swiss-Prot : SWS_FT_FI4 23) chain B residue 402 type BINDING sequence S description BINDING => ECO:0000269|PubMed:9519410, ECO:0007744|PDB:1A3W source Swiss-Prot : SWS_FT_FI4 24) chain B residue 240 type SITE sequence K description Transition state stabilizer => ECO:0000269|PubMed:10413488 source Swiss-Prot : SWS_FT_FI5 25) chain B residue 9 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI7 26) chain B residue 16 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI8 27) chain B residue 31 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI9 28) chain B residue 184 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI9 29) chain B residue 2 type MOD_RES sequence S description N-acetylserine => ECO:0007744|PubMed:17287358 source Swiss-Prot : SWS_FT_FI6 30) chain B residue 70 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI10 31) chain B residue 316 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI10 32) chain B residue 213 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17287358 source Swiss-Prot : SWS_FT_FI11 33) chain B residue 478 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI12 34) chain B 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 35) chain B 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 36) chain B 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 37) chain B 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 38) chain B 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 39) chain B 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 40) chain B 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 41) chain B 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 42) chain B 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 43) chain B 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 44) chain B 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 45) chain B 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

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