eF-site ID 2ik6-AB PDB Code 2ik6 Chain A, B click to enlarge Title Yeast inorganic pyrophosphatase variant D120E 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 RNCFPHHGYIHNYGAFPQTWEDPGDNDPIEVLEIGETIAY TGQVKQVKALGIMALLDEGETDWKVIAIDINDPLAPKLND IEDVEKYFPGLLRATNEWFRIYKIPDGKPENQFAFSGEAK NKKYALDIIKETHDSWKQLIAGSKGIDLTNVTLPDTPTYS KAASDAIPPASLKADAPIDKSIDKWFFI B:  TYTTRQIGAKNTLEYKVYIEKDGKPVSAFHDIPLYADKEN NIFNMVVEIPRWTNAKLEITKEETLNPIIQDTKKGKLRFV RNCFPHHGYIHNYGAFPQTWEDPNVSHPETKAVGDNDPIE VLEIGETIAYTGQVKQVKALGIMALLDEGETDWKVIAIDI NDPLAPKLNDIEDVEKYFPGLLRATNEWFRIYKIPDGKPE NQFAFSGEAKNKKYALDIIKETHDSWKQLIAGKSSDSKGI DLTNVTLPDTPTYSKAASDAIPPASLKADAPIDKSIDKWF FI Description Functional site 1) chain A residue 115 type sequence D description BINDING SITE FOR RESIDUE MG A 287 source : AC1 2) chain A residue 120 type sequence E 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 B residue 115 type sequence D description BINDING SITE FOR RESIDUE MG B 287 source : AC3 5) chain B residue 120 type sequence E description BINDING SITE FOR RESIDUE MG B 287 source : AC3 6) chain B residue 152 type sequence D description BINDING SITE FOR RESIDUE MG B 287 source : AC3 7) chain B residue 78 type sequence R description BINDING SITE FOR RESIDUE PO4 B 290 source : AC6 8) chain B residue 147 type sequence D description BINDING SITE FOR RESIDUE PO4 B 290 source : AC6 9) chain B residue 192 type sequence Y description BINDING SITE FOR RESIDUE PO4 B 290 source : AC6 10) chain B residue 193 type sequence K description BINDING SITE FOR RESIDUE PO4 B 290 source : AC6 11) chain A residue 78 type sequence R description BINDING SITE FOR RESIDUE PO4 A 289 source : AC7 12) chain A residue 147 type sequence D description BINDING SITE FOR RESIDUE PO4 A 289 source : AC7 13) chain A residue 192 type sequence Y description BINDING SITE FOR RESIDUE PO4 A 289 source : AC7 14) chain A residue 193 type sequence K description BINDING SITE FOR RESIDUE PO4 A 289 source : AC7 15) chain B residue 186 type sequence N description BINDING SITE FOR RESIDUE MPD B 291 source : AC8 16) chain B residue 206 type sequence S description BINDING SITE FOR RESIDUE MPD B 291 source : AC8 17) chain B residue 207 type sequence G description BINDING SITE FOR RESIDUE MPD B 291 source : AC8 18) chain A residue 79 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 19) chain A residue 116 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 20) chain A residue 121 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2 21) chain A residue 153 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI2 22) chain B residue 79 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 23) chain B residue 116 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 24) chain B residue 121 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2 25) chain B residue 153 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI2 26) chain A residue 65 type MOD_RES sequence L description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 27) chain B residue 65 type MOD_RES sequence L description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 28) 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 29) 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 30) chain A residue 90 type ACT_SITE sequence I description Proton donor => ECO:0000269|PubMed:1322842 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 90 type ACT_SITE sequence I description Proton donor => ECO:0000269|PubMed:1322842 source Swiss-Prot : SWS_FT_FI1 32) 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 33) 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 34) 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 35) 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 36) 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 37) 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

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