eF-site ID 1m38-AB PDB Code 1m38 Chain A, B click to enlarge Title Structure of Inorganic Pyrophosphatase Classification HYDROLASE Compound INORGANIC PYROPHOSPHATASE Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence A:  TYTTRQIGAKNTLEYKVYIEKDGKPVSAFHDIPLYADKEN NIFNMVVEIPRWTNAKLEITKEETLNPIIQDTKKGKLRFV RNCFPHHGYIHNYGAFPQTWEDPNVSHPETKAVGDNDPID VLEIGETIAYTGQVKQVKALGIMALLDEGETDWKVIAIDI NDPLAPKLNDIEDVEKYFPGLLRATNEWFRIYKIPDGKPE NQFAFSGEAKNKKYALDIIKETHDSWKQLIAGKSSDSKGI DLTNVTLPDTPTYSKAASDAIPPASPKADAPIDKSIDKWF FI B:  TYTTRQIGAKNTLEYKVYIEKDGKPVSAFHDIPLYADKEN NIFNMVVEIPRWTNAKLEITKEETLNPIIQDTKKGKLRFV RNCFPHHGYIHNYGAFPQTWEDPNVSHPETKAVGDNDPID VLEIGETIAYTGQVKQVKALGIMALLDEGETDWKVIAIDI NDPLAPKLNDIEDVEKYFPGLLRATNEWFRIYKIPDGKPE NQFAFSGEAKNKKYALDIIKETHDSWKQLIAGKSSDSKGI DLTNVTLPDTPTYSKAASDAIPPASPKADAPIDKSIDKWF FI Description Functional site 1) chain A residue 115 type sequence D description BINDING SITE FOR RESIDUE CO A 401 source : AC1 2) chain A residue 120 type sequence D description BINDING SITE FOR RESIDUE CO A 401 source : AC1 3) chain A residue 152 type sequence D description BINDING SITE FOR RESIDUE CO A 401 source : AC1 4) chain A residue 120 type sequence D description BINDING SITE FOR RESIDUE CO A 402 source : AC2 5) chain A residue 56 type sequence K description BINDING SITE FOR RESIDUE CO A 403 source : AC3 6) chain A residue 58 type sequence E description BINDING SITE FOR RESIDUE CO A 403 source : AC3 7) chain A residue 147 type sequence D description BINDING SITE FOR RESIDUE CO A 404 source : AC4 8) chain A residue 152 type sequence D description BINDING SITE FOR RESIDUE CO A 404 source : AC4 9) chain B residue 115 type sequence D description BINDING SITE FOR RESIDUE CO B 401 source : AC5 10) chain B residue 120 type sequence D description BINDING SITE FOR RESIDUE CO B 401 source : AC5 11) chain B residue 152 type sequence D description BINDING SITE FOR RESIDUE CO B 401 source : AC5 12) chain B residue 120 type sequence D description BINDING SITE FOR RESIDUE CO B 402 source : AC6 13) chain A residue 74 type sequence K description BINDING SITE FOR RESIDUE PO4 B 3501 source : AC7 14) chain B residue 56 type sequence K description BINDING SITE FOR RESIDUE PO4 B 3501 source : AC7 15) chain B residue 78 type sequence R description BINDING SITE FOR RESIDUE PO4 B 3501 source : AC7 16) chain B residue 147 type sequence D description BINDING SITE FOR RESIDUE PO4 B 3501 source : AC7 17) chain B residue 192 type sequence Y description BINDING SITE FOR RESIDUE PO4 B 3501 source : AC7 18) chain B residue 193 type sequence K description BINDING SITE FOR RESIDUE PO4 B 3501 source : AC7 19) chain A residue 56 type sequence K description BINDING SITE FOR RESIDUE PO4 A 3301 source : AC8 20) chain A residue 58 type sequence E description BINDING SITE FOR RESIDUE PO4 A 3301 source : AC8 21) chain A residue 93 type sequence Y description BINDING SITE FOR RESIDUE PO4 A 3301 source : AC8 22) chain A residue 115 type sequence D description BINDING SITE FOR RESIDUE PO4 A 3301 source : AC8 23) chain A residue 117 type sequence D description BINDING SITE FOR RESIDUE PO4 A 3301 source : AC8 24) chain A residue 120 type sequence D description BINDING SITE FOR RESIDUE PO4 A 3301 source : AC8 25) chain A residue 152 type sequence D description BINDING SITE FOR RESIDUE PO4 A 3301 source : AC8 26) chain B residue 89 type ACT_SITE sequence Y description Proton donor => ECO:0000269|PubMed:1322842 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 89 type ACT_SITE sequence Y description Proton donor => ECO:0000269|PubMed:1322842 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 115-121 type prosite sequence DNDPIDV description PPASE Inorganic pyrophosphatase signature. DNDPIDV source prosite : PS00387 29) chain B residue 265 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 30) chain A residue 265 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 31) chain A residue 238 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI7 32) chain A residue 278 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI7 33) chain B residue 238 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI7 34) chain B residue 278 type CROSSLNK sequence K 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 152 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 36) chain B residue 78 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 37) chain B residue 115 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 38) chain B residue 120 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 39) chain B residue 152 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 40) chain A residue 78 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 41) chain A residue 115 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 42) chain A residue 120 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 43) chain B residue 64 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 44) chain A residue 64 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 45) chain B residue 250 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI4 46) chain A residue 250 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI4

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