eF-site ID 117e-AB PDB Code 117e Chain A, B 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 B:  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 B residue 1117 type sequence E description source : MN5 11) chain B residue 1152 type sequence D description source : MN5 12) chain B residue 1115 type sequence D description source : MN5 13) chain B residue 1120 type sequence D description source : MN5 14) chain B residue 1117 type sequence E description source : MN6 15) chain B residue 1093 type sequence Y description source : MN6 16) chain B residue 1120 type sequence D description source : MN6 17) chain B residue 1152 type sequence D description source : MN8 18) chain B residue 1147 type sequence D description source : MN8 19) chain A residue 115 type sequence D description BINDING SITE FOR RESIDUE MN A 2001 source : AC1 20) chain A residue 117 type sequence E description BINDING SITE FOR RESIDUE MN A 2001 source : AC1 21) chain A residue 120 type sequence D description BINDING SITE FOR RESIDUE MN A 2001 source : AC1 22) chain A residue 152 type sequence D description BINDING SITE FOR RESIDUE MN A 2001 source : AC1 23) chain A residue 117 type sequence E description BINDING SITE FOR RESIDUE MN A 2002 source : AC2 24) chain A residue 120 type sequence D description BINDING SITE FOR RESIDUE MN A 2002 source : AC2 25) chain A residue 147 type sequence D description BINDING SITE FOR RESIDUE MN A 2004 source : AC4 26) chain A residue 152 type sequence D description BINDING SITE FOR RESIDUE MN A 2004 source : AC4 27) chain B residue 1115 type sequence D description BINDING SITE FOR RESIDUE MN B 2005 source : AC5 28) chain B residue 1117 type sequence E description BINDING SITE FOR RESIDUE MN B 2005 source : AC5 29) chain B residue 1120 type sequence D description BINDING SITE FOR RESIDUE MN B 2005 source : AC5 30) chain B residue 1152 type sequence D description BINDING SITE FOR RESIDUE MN B 2005 source : AC5 31) chain B residue 1117 type sequence E description BINDING SITE FOR RESIDUE MN B 2006 source : AC6 32) chain B residue 1120 type sequence D description BINDING SITE FOR RESIDUE MN B 2006 source : AC6 33) chain B residue 1058 type sequence E description BINDING SITE FOR RESIDUE MN B 2007 source : AC7 34) chain B residue 1117 type sequence E description BINDING SITE FOR RESIDUE MN B 2007 source : AC7 35) chain B residue 1147 type sequence D description BINDING SITE FOR RESIDUE MN B 2008 source : AC8 36) chain B residue 1152 type sequence D description BINDING SITE FOR RESIDUE MN B 2008 source : AC8 37) chain A residue 56 type sequence K description BINDING SITE FOR RESIDUE PO4 A 3001 source : AC9 38) chain A residue 78 type sequence R description BINDING SITE FOR RESIDUE PO4 A 3001 source : AC9 39) chain A residue 147 type sequence D description BINDING SITE FOR RESIDUE PO4 A 3001 source : AC9 40) chain A residue 192 type sequence Y description BINDING SITE FOR RESIDUE PO4 A 3001 source : AC9 41) chain A residue 193 type sequence K description BINDING SITE FOR RESIDUE PO4 A 3001 source : AC9 42) chain A residue 56 type sequence K description BINDING SITE FOR RESIDUE PO4 A 3002 source : BC1 43) chain A residue 93 type sequence Y description BINDING SITE FOR RESIDUE PO4 A 3002 source : BC1 44) chain A residue 115 type sequence D description BINDING SITE FOR RESIDUE PO4 A 3002 source : BC1 45) chain A residue 117 type sequence E description BINDING SITE FOR RESIDUE PO4 A 3002 source : BC1 46) chain A residue 120 type sequence D description BINDING SITE FOR RESIDUE PO4 A 3002 source : BC1 47) chain A residue 152 type sequence D description BINDING SITE FOR RESIDUE PO4 A 3002 source : BC1 48) chain B residue 1056 type sequence K description BINDING SITE FOR RESIDUE PO4 B 3004 source : BC2 49) chain B residue 1093 type sequence Y description BINDING SITE FOR RESIDUE PO4 B 3004 source : BC2 50) chain B residue 1115 type sequence D description BINDING SITE FOR RESIDUE PO4 B 3004 source : BC2 51) chain B residue 1117 type sequence E description BINDING SITE FOR RESIDUE PO4 B 3004 source : BC2 52) chain B residue 1120 type sequence D description BINDING SITE FOR RESIDUE PO4 B 3004 source : BC2 53) chain B residue 1152 type sequence D description BINDING SITE FOR RESIDUE PO4 B 3004 source : BC2 54) chain B residue 1154 type sequence K description BINDING SITE FOR RESIDUE PO4 B 3004 source : BC2 55) chain A residue 90 type ACT_SITE sequence I description Proton donor => ECO:0000269|PubMed:1322842 source Swiss-Prot : SWS_FT_FI1 56) chain B residue 1090 type ACT_SITE sequence I description Proton donor => ECO:0000269|PubMed:1322842 source Swiss-Prot : SWS_FT_FI1 57) chain A residue 79 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 58) chain A residue 116 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 59) chain A residue 121 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2 60) chain A residue 153 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI2 61) chain B residue 1079 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 62) chain B residue 1116 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 63) chain B residue 1121 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2 64) chain B residue 1153 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI2 65) chain A residue 65 type MOD_RES sequence L description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 66) chain B residue 1065 type MOD_RES sequence L description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 67) 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 68) chain B residue 1251 type MOD_RES sequence P description Phosphothreonine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI4 69) 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 70) chain B residue 1266 type MOD_RES sequence L description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 71) 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 72) 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 73) chain B residue 1239 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 74) chain B residue 1279 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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