eF-site ID 117e-A PDB Code 117e Chain A click to enlarge Title THE R78K AND D117E ACTIVE SITE VARIANTS OF SACCHAROMYCES CEREVISIAE SOLUBLE INORGANIC PYROPHOSPHATASE: STRUCTURAL STUDIES AND MECHANISTIC IMPLICATIONS Classification HYDROLASE Compound PROTEIN (INORGANIC PYROPHOSPHATASE) Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (IPYR_YEAST) Sequence A:  TYTTRQIGAKNTLEYKVYIEKDGKPVSAFHDIPLYADKEN NIFNMVVEIPRWTNAKLEITKEETLNPIIQDTKKGKLRFV RNCFPHHGYIHNYGAFPQTWEDPNVSHPETKAVGDNEPID VLEIGETIAYTGQVKQVKALGIMALLDEGETDWKVIAIDI NDPLAPKLNDIEDVEKYFPGLLRATNEWFRIYKIPDGKPE NQFAFSGEAKNKKYALDIIKETHDSWKQLIAGKSSDSKGI DLTNVTLPDTPTYSKAASDAIPPASLKADAPIDKSIDKWF FI Description Functional site 1) chain A residue 117 type sequence E description source : MN1 2) chain A residue 152 type sequence D description source : MN1 3) chain A residue 115 type sequence D description source : MN1 4) chain A residue 120 type sequence D description source : MN1 5) chain A residue 117 type sequence E description source : MN2 6) chain A residue 93 type sequence Y description source : MN2 7) chain A residue 120 type sequence D description source : MN2 8) chain A residue 152 type sequence D description source : MN4 9) chain A residue 147 type sequence D description source : MN4 10) chain A residue 115 type sequence D description BINDING SITE FOR RESIDUE MN A 2001 source : AC1 11) chain A residue 117 type sequence E description BINDING SITE FOR RESIDUE MN A 2001 source : AC1 12) chain A residue 120 type sequence D description BINDING SITE FOR RESIDUE MN A 2001 source : AC1 13) chain A residue 152 type sequence D description BINDING SITE FOR RESIDUE MN A 2001 source : AC1 14) chain A residue 117 type sequence E description BINDING SITE FOR RESIDUE MN A 2002 source : AC2 15) chain A residue 120 type sequence D description BINDING SITE FOR RESIDUE MN A 2002 source : AC2 16) chain A residue 147 type sequence D description BINDING SITE FOR RESIDUE MN A 2004 source : AC4 17) chain A residue 152 type sequence D description BINDING SITE FOR RESIDUE MN A 2004 source : AC4 18) chain A residue 56 type sequence K description BINDING SITE FOR RESIDUE PO4 A 3001 source : AC9 19) chain A residue 78 type sequence R description BINDING SITE FOR RESIDUE PO4 A 3001 source : AC9 20) chain A residue 147 type sequence D description BINDING SITE FOR RESIDUE PO4 A 3001 source : AC9 21) chain A residue 192 type sequence Y description BINDING SITE FOR RESIDUE PO4 A 3001 source : AC9 22) chain A residue 193 type sequence K description BINDING SITE FOR RESIDUE PO4 A 3001 source : AC9 23) chain A residue 56 type sequence K description BINDING SITE FOR RESIDUE PO4 A 3002 source : BC1 24) chain A residue 93 type sequence Y description BINDING SITE FOR RESIDUE PO4 A 3002 source : BC1 25) chain A residue 115 type sequence D description BINDING SITE FOR RESIDUE PO4 A 3002 source : BC1 26) chain A residue 117 type sequence E description BINDING SITE FOR RESIDUE PO4 A 3002 source : BC1 27) chain A residue 120 type sequence D description BINDING SITE FOR RESIDUE PO4 A 3002 source : BC1 28) chain A residue 152 type sequence D description BINDING SITE FOR RESIDUE PO4 A 3002 source : BC1 29) chain A residue 90 type ACT_SITE sequence I description Proton donor => ECO:0000269|PubMed:1322842 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 79 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 31) chain A residue 116 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 32) chain A residue 121 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2 33) chain A residue 153 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI2 34) chain A residue 65 type MOD_RES sequence L description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 35) chain A residue 251 type MOD_RES sequence P description Phosphothreonine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI4 36) chain A residue 266 type MOD_RES sequence L description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 37) chain A residue 239 type CROSSLNK sequence G description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI7 38) chain A residue 279 type CROSSLNK sequence W description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI7

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