eF-site ID 2ik2-AB PDB Code 2ik2 Chain A, B click to enlarge Title Yeast inorganic pyrophosphatase variant D115E with magnesium and phosphate Classification HYDROLASE Compound Inorganic pyrophosphatase Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (IPYR_YEAST) Sequence A:  TYTTRQIGAKNTLEYKVYIEKDGKPVSAFHDIPLYADKEN NIFNMVVEIPRWTNAKLEITKEETLNPIIQDTKKGKLRFV RNCFPHHGYIHNYGAFPQTWEDPNVSHGENDPIDVLEIGE TIAYTGQVKQVKALGIMALLDEGETDWKVIAIDINDPLAP KLNDIEDVEKYFPGLLRATNEWFRIYKIPDGKPENQFAFS GEAKNKKYALDIIKETHDSWKQLIAGKSSDSKGIDLTNVT LPDTPTYSKAASDAIPPASLKADAPIDKSIDKWFFI B:  TYTTRQIGAKNTLEYKVYIEKDGKPVSAFHDIPLYADKEN NIFNMVVEIPRWTNAKLEITKEETLNPIIQDTKKGKLRFV RNCFPHHGYIHNYGAFPQTWEDPNVSHPETKAVGENDPID VLEIGETIAYTGQVKQVKALGIMALLDEGETDWKVIAIDI NDPLAPKLNDIEDVEKYFPGLLRATNEWFRIYKIPDGKPE NQFAFSGEAKNKKYALDIIKETHDSWKQLIAGKSSDSKGI DLTNVTLPDTPTYSKAASDAIPPASLKADAPIDKSIDKWF FI Description Functional site 1) chain A residue 115 type sequence E description BINDING SITE FOR RESIDUE MG A 287 source : AC1 2) chain A residue 120 type sequence D description BINDING SITE FOR RESIDUE MG A 287 source : AC1 3) chain A residue 152 type sequence D description BINDING SITE FOR RESIDUE MG A 287 source : AC1 4) chain A residue 120 type sequence D description BINDING SITE FOR RESIDUE MG A 288 source : AC2 5) chain A residue 58 type sequence E description BINDING SITE FOR RESIDUE MG A 289 source : AC3 6) chain A residue 147 type sequence D description BINDING SITE FOR RESIDUE MG A 290 source : AC4 7) chain A residue 152 type sequence D description BINDING SITE FOR RESIDUE MG A 290 source : AC4 8) chain B residue 115 type sequence E description BINDING SITE FOR RESIDUE MG B 287 source : AC5 9) chain B residue 120 type sequence D description BINDING SITE FOR RESIDUE MG B 287 source : AC5 10) chain B residue 152 type sequence D description BINDING SITE FOR RESIDUE MG B 287 source : AC5 11) chain B residue 120 type sequence D description BINDING SITE FOR RESIDUE MG B 288 source : AC6 12) chain B residue 58 type sequence E description BINDING SITE FOR RESIDUE MG B 289 source : AC7 13) chain B residue 115 type sequence E description BINDING SITE FOR RESIDUE MG B 290 source : AC8 14) chain B residue 147 type sequence D description BINDING SITE FOR RESIDUE MG B 290 source : AC8 15) chain B residue 152 type sequence D description BINDING SITE FOR RESIDUE MG B 290 source : AC8 16) chain B residue 56 type sequence K description BINDING SITE FOR RESIDUE PO4 B 291 source : AC9 17) chain B residue 58 type sequence E description BINDING SITE FOR RESIDUE PO4 B 291 source : AC9 18) chain B residue 93 type sequence Y description BINDING SITE FOR RESIDUE PO4 B 291 source : AC9 19) chain B residue 115 type sequence E description BINDING SITE FOR RESIDUE PO4 B 291 source : AC9 20) chain B residue 117 type sequence D description BINDING SITE FOR RESIDUE PO4 B 291 source : AC9 21) chain B residue 120 type sequence D description BINDING SITE FOR RESIDUE PO4 B 291 source : AC9 22) chain B residue 152 type sequence D description BINDING SITE FOR RESIDUE PO4 B 291 source : AC9 23) chain B residue 154 type sequence K description BINDING SITE FOR RESIDUE PO4 B 291 source : AC9 24) chain B residue 56 type sequence K description BINDING SITE FOR RESIDUE PO4 B 292 source : BC1 25) chain B residue 58 type sequence E description BINDING SITE FOR RESIDUE PO4 B 292 source : BC1 26) chain B residue 78 type sequence R description BINDING SITE FOR RESIDUE PO4 B 292 source : BC1 27) chain B residue 115 type sequence E description BINDING SITE FOR RESIDUE PO4 B 292 source : BC1 28) chain B residue 147 type sequence D description BINDING SITE FOR RESIDUE PO4 B 292 source : BC1 29) chain B residue 192 type sequence Y description BINDING SITE FOR RESIDUE PO4 B 292 source : BC1 30) chain B residue 193 type sequence K description BINDING SITE FOR RESIDUE PO4 B 292 source : BC1 31) chain A residue 58 type sequence E description BINDING SITE FOR RESIDUE PO4 A 291 source : BC2 32) chain A residue 78 type sequence R description BINDING SITE FOR RESIDUE PO4 A 291 source : BC2 33) chain A residue 192 type sequence Y description BINDING SITE FOR RESIDUE PO4 A 291 source : BC2 34) chain A residue 193 type sequence K description BINDING SITE FOR RESIDUE PO4 A 291 source : BC2 35) chain A residue 56 type sequence K description BINDING SITE FOR RESIDUE PO4 A 292 source : BC3 36) chain A residue 58 type sequence E description BINDING SITE FOR RESIDUE PO4 A 292 source : BC3 37) chain A residue 93 type sequence Y description BINDING SITE FOR RESIDUE PO4 A 292 source : BC3 38) chain A residue 120 type sequence D description BINDING SITE FOR RESIDUE PO4 A 292 source : BC3 39) chain A residue 152 type sequence D description BINDING SITE FOR RESIDUE PO4 A 292 source : BC3 40) chain A residue 154 type sequence K description BINDING SITE FOR RESIDUE PO4 A 292 source : BC3 41) chain A residue 90 type ACT_SITE sequence I description Proton donor => ECO:0000269|PubMed:1322842 source Swiss-Prot : SWS_FT_FI1 42) chain B residue 90 type ACT_SITE sequence I description Proton donor => ECO:0000269|PubMed:1322842 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 65 type MOD_RES sequence L description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 44) chain B residue 65 type MOD_RES sequence L description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 45) 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 46) chain B residue 251 type MOD_RES sequence P description Phosphothreonine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI4 47) 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 48) chain B residue 266 type MOD_RES sequence L description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 49) 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 50) 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 51) chain B 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 52) chain B 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 53) chain A residue 79 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 54) chain A residue 116 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 55) chain A residue 121 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2 56) chain A residue 153 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI2 57) chain B residue 79 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 58) chain B residue 116 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 59) chain B residue 121 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2 60) chain B residue 153 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI2

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