eF-site ID 1pnt-A PDB Code 1pnt Chain A click to enlarge Title CRYSTAL STRUCTURE OF BOVINE HEART PHOSPHOTYROSYL PHOSPHATASE AT 2.2 ANGSTROMS RESOLUTION Classification HYDROLASE Compound ACID PHOSPHATASE Source (PPAC_BOVIN) Sequence A:  AEQVTKSVLFVCLGNICRSPIAEAVFRKLVTDQNISDNWV IDSGAVSDWNVGRSPDPRAVSCLRNHGINTAHKARQVTKE DFVTFDYILCMDESNLRDLNRKSNQVKNCRAKIELLGSYD PQKQLIIEDPYYGNDADFETVYQQCVRCCRAFLEKVR Description Functional site 1) chain A residue 12 type sequence C description ACTIVE SITE source : ACT 2) chain A residue 13 type sequence L description ACTIVE SITE source : ACT 3) chain A residue 14 type sequence G description ACTIVE SITE source : ACT 4) chain A residue 15 type sequence N description ACTIVE SITE source : ACT 5) chain A residue 16 type sequence I description ACTIVE SITE source : ACT 6) chain A residue 17 type sequence C description ACTIVE SITE source : ACT 7) chain A residue 18 type sequence R description ACTIVE SITE source : ACT 8) chain A residue 19 type sequence S description ACTIVE SITE source : ACT 9) chain A residue 12 type sequence C description BINDING SITE FOR RESIDUE PO4 A 158 source : AC1 10) chain A residue 13 type sequence L description BINDING SITE FOR RESIDUE PO4 A 158 source : AC1 11) chain A residue 14 type sequence G description BINDING SITE FOR RESIDUE PO4 A 158 source : AC1 12) chain A residue 15 type sequence N description BINDING SITE FOR RESIDUE PO4 A 158 source : AC1 13) chain A residue 16 type sequence I description BINDING SITE FOR RESIDUE PO4 A 158 source : AC1 14) chain A residue 17 type sequence C description BINDING SITE FOR RESIDUE PO4 A 158 source : AC1 15) chain A residue 18 type sequence R description BINDING SITE FOR RESIDUE PO4 A 158 source : AC1 16) chain A residue 129 type sequence D description BINDING SITE FOR RESIDUE PO4 A 158 source : AC1 17) chain A residue 130 type ACT_SITE sequence P description Proton donor => ECO:0000269|PubMed:8052313 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 2 type MOD_RES sequence E description N-acetylalanine => ECO:0000269|PubMed:2644264 source Swiss-Prot : SWS_FT_FI4 19) chain A residue 132 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P24666 source Swiss-Prot : SWS_FT_FI5 20) chain A residue 133 type MOD_RES sequence G description Phosphotyrosine => ECO:0000250|UniProtKB:P24666 source Swiss-Prot : SWS_FT_FI5 21) chain A residue 13 type catalytic sequence L description 462 source MCSA : MCSA1 22) chain A residue 16 type catalytic sequence I description 462 source MCSA : MCSA1 23) chain A residue 18 type catalytic sequence R description 462 source MCSA : MCSA1 24) chain A residue 19 type catalytic sequence S description 462 source MCSA : MCSA1 25) chain A residue 20 type catalytic sequence P description 462 source MCSA : MCSA1 26) chain A residue 130 type catalytic sequence P description 462 source MCSA : MCSA1 27) chain A residue 13 type ACT_SITE sequence L description Nucleophile => ECO:0000269|PubMed:8052313, ECO:0000269|PubMed:8132604, ECO:0000269|PubMed:8319676 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 19 type ACT_SITE sequence S description ACT_SITE => ECO:0000269|PubMed:8052313, ECO:0000269|PubMed:8319676 source Swiss-Prot : SWS_FT_FI2

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