eF-site ID 2npp-ABC PDB Code 2npp Chain A, B, C click to enlarge Title Structure of the Protein Phosphatase 2A Holoenzyme Classification HYDROLASE/HYDROLASE INHIBITOR Compound Protein Phosphatase 2, regulatory subunit A (PR 65), alpha isoform Source Homo sapiens (Human) (NOR00109) Sequence A:  DSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERT RSELLPFLTDTIYDEDEVLLALAEQLGTFTTLVGGPEYVH CLLPPLESLATVEETVVRDKAVESLRAISHEHSPSDLEAH FVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELR QYFRNLCSDDTPMVRRAAASKLGEFAKVLELDNVKSEIIP MFSNLASDEQDSVRLLAVEACVNIAQLLPQEDLEALVMPT LRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAF QNLMKDCEAEVRAAASHKVKEFCENLSADCRENVIMSQIL PCIKELVSDANQHVKSALASVIMGLSPILGKDNTIEHLLP LFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPA IVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLC MAWLVDHVYAIREAATSNLKKLVEKFGKEWAHATIIPKVL AMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLR MAGDPVANVRFNVAKSLQKIGPILDNSTLQSEVKPILEKL TQDQDVDVKYFAQEALTVLSLA B:  QEKLFIQKLRQCCVLFDFVSDPLSDLKWKEVKRAALSEMV EYITHNRNVITEPIYPEVVHMFAVNMFRTLPPSSNPTGAE FDPEEDEPTLEAAWPHLQLVYEFFLRFLESPDFQPNIAKK YIDQKFVLQLLELFDSEDPRERDFLKTTLHRIYGKFLGLR AYIRKQINNIFYRFIYETEHHNGIAELLEILGSIINGFAL PLKEEHKIFLLKVLLPLHKVKSLSVYHPQLAYCVVQFLEK DSTLTEPVVMALLKYWPKTHSPKEVMFLNELEEILDVIEP SEFVKIMEPLFRQLAKCVSSPHFQVAERALYYWNNEYIMS LISDNAAKILPIMFPSLYRNSKTHWNKTIHGLIYNALKLF MEMNQKLFDDCTQQFKAEKLKEKLKMKE C:  DEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTK ESNVQEVRCPVTVCGDVHGQFHDLMELFRIGGKSPDTNYL FMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHESR QITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDG QIFCLHGGLSPSIDTLDHIRALDRLQEVPHEGPMCDLLWS DPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRAH QLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDT LKYSFLQFDPAPRRGEPHVTRRTPDYFL Description Functional site 1) chain C residue 57 type sequence D description BINDING SITE FOR RESIDUE MN C 501 source : AC1 2) chain C residue 85 type sequence D description BINDING SITE FOR RESIDUE MN C 501 source : AC1 3) chain C residue 117 type sequence N description BINDING SITE FOR RESIDUE MN C 501 source : AC1 4) chain C residue 167 type sequence H description BINDING SITE FOR RESIDUE MN C 501 source : AC1 5) chain C residue 241 type sequence H description BINDING SITE FOR RESIDUE MN C 501 source : AC1 6) chain C residue 57 type sequence D description BINDING SITE FOR RESIDUE MN C 502 source : AC2 7) chain C residue 59 type sequence H description BINDING SITE FOR RESIDUE MN C 502 source : AC2 8) chain C residue 85 type sequence D description BINDING SITE FOR RESIDUE MN C 502 source : AC2 9) chain C residue 57 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17055435 source Swiss-Prot : SWS_FT_FI2 10) chain C residue 59 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17055435 source Swiss-Prot : SWS_FT_FI2 11) chain C residue 85 type BINDING sequence D description BINDING => ECO:0000269|PubMed:17055435 source Swiss-Prot : SWS_FT_FI2 12) chain C residue 117 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17055435 source Swiss-Prot : SWS_FT_FI2 13) chain C residue 167 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17055435 source Swiss-Prot : SWS_FT_FI2 14) chain C residue 241 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17055435 source Swiss-Prot : SWS_FT_FI2 15) chain C residue 307 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P67774 source Swiss-Prot : SWS_FT_FI3 16) chain C residue 309 type MOD_RES sequence L description Leucine methyl ester => ECO:0000269|PubMed:8206937 source Swiss-Prot : SWS_FT_FI4 17) chain C residue 114-119 type prosite sequence LRGNHE description SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE source prosite : PS00125

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