eF-site ID 1ypp-A PDB Code 1ypp Chain A click to enlarge Title ACID ANHYDRIDE HYDROLASE Classification HYDROLASE Compound INORGANIC PYROPHOSPHATASE Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence A:  TYTTRQIGAKNTLEYKVYIEKDGKPVSAFHDIPLYADKEN NIFNMVVEIPRWTNAKLEITKEETLNPIIQDTAKGKLRFV RNCFPHHGYIHNYGAFPQTWEDPNVSHPETKAVGDNDPID VLEIGETIAYTGQVKQVKALGIMALLDEGETDWKVIAIDI NDPLAPKLNDIEDVEKYFPGLLRATNEWFRIYKIPDGKPE NQFAFSGEAKNKKYALDIIKETHDSWKQLIAGKSSDSKGI DLTNVTLPDTPTYSKAASDAIPPASPKADAPIDKSIDKWF FI Description Functional site 1) chain A residue 115 type sequence D description BINDING SITE FOR RESIDUE MN A 401 source : AC1 2) chain A residue 120 type sequence D description BINDING SITE FOR RESIDUE MN A 401 source : AC1 3) chain A residue 152 type sequence D description BINDING SITE FOR RESIDUE MN A 401 source : AC1 4) chain A residue 120 type sequence D description BINDING SITE FOR RESIDUE MN A 402 source : AC2 5) chain A residue 147 type sequence D description BINDING SITE FOR RESIDUE MN A 403 source : AC3 6) chain A residue 152 type sequence D description BINDING SITE FOR RESIDUE MN A 403 source : AC3 7) chain A residue 58 type sequence E description BINDING SITE FOR RESIDUE MN A 404 source : AC4 8) chain A residue 56 type sequence K description BINDING SITE FOR RESIDUE PO4 A 301 source : AC5 9) chain A residue 58 type sequence E description BINDING SITE FOR RESIDUE PO4 A 301 source : AC5 10) chain A residue 78 type sequence R description BINDING SITE FOR RESIDUE PO4 A 301 source : AC5 11) chain A residue 147 type sequence D description BINDING SITE FOR RESIDUE PO4 A 301 source : AC5 12) chain A residue 192 type sequence Y description BINDING SITE FOR RESIDUE PO4 A 301 source : AC5 13) chain A residue 193 type sequence K description BINDING SITE FOR RESIDUE PO4 A 301 source : AC5 14) chain A residue 56 type sequence K description BINDING SITE FOR RESIDUE PO4 A 302 source : AC6 15) chain A residue 58 type sequence E description BINDING SITE FOR RESIDUE PO4 A 302 source : AC6 16) chain A residue 93 type sequence Y description BINDING SITE FOR RESIDUE PO4 A 302 source : AC6 17) chain A residue 115 type sequence D description BINDING SITE FOR RESIDUE PO4 A 302 source : AC6 18) chain A residue 117 type sequence D description BINDING SITE FOR RESIDUE PO4 A 302 source : AC6 19) chain A residue 120 type sequence D description BINDING SITE FOR RESIDUE PO4 A 302 source : AC6 20) chain A residue 152 type sequence D description BINDING SITE FOR RESIDUE PO4 A 302 source : AC6 21) chain A residue 90 type ACT_SITE sequence I description Proton donor => ECO:0000269|PubMed:1322842 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 266 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 23) 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 24) 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 25) chain A residue 115-121 type prosite sequence DNDPIDV description PPASE Inorganic pyrophosphatase signature. DNDPIDV source prosite : PS00387 26) chain A residue 79 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI2 27) chain A residue 116 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 28) chain A residue 121 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2 29) chain A residue 153 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI2 30) chain A residue 65 type MOD_RES sequence L description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 31) 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

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