eF-site ID 1xl0-A PDB Code 1xl0 Chain A click to enlarge Title Kinetic and crystallographic studies on 2-(beta-D-glucopyranosyl)-5-methyl-1,3,4-oxadiazole,-benzothiazole, and-benzimidazole, inhibitors of muscle glycogen phosphorylase b. Evidence for a new binding site. Classification TRANSFERASE Compound Glycogen phosphorylase, muscle form Source ORGANISM_COMMON: rabbit; ORGANISM_SCIENTIFIC: Oryctolagus cuniculus; Sequence A:  QISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDY YFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYM GRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGL GNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIC GGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQ GAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPND FNLGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEY FVVAATLQDIIRRFKSSTNFDAFPDKVAIQLNDTHPSLAI PELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVLPEALER WPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLR RMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKT IFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEIIAER IGEEYISDLDQLRKLLSYVDDEAFIRDVAKVKQENKLKFA AYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHVITL YNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITAI GDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQI STAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEE NFFIFGMRVEDVDRLDQRGYNAQEYYDRIPELRQIIEQLS SGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVKCQER VSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWG VEPSRQRLPA Description (1)  Glycogen phosphorylase, muscle form (E.C.2.4.1.1) Functional site 1) chain A residue 514 type MOD_RES sequence D description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 2) chain A residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 3) chain A residue 748 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 4) chain A residue 681 type MOD_RES sequence F description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:7500360, ECO:0000269|PubMed:8976550, ECO:0007744|PDB:2PRI, ECO:0007744|PDB:2SKC, ECO:0007744|PDB:2SKD, ECO:0007744|PDB:2SKE source Swiss-Prot : SWS_FT_FI11 5) chain A residue 43 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 6) chain A residue 310 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 7) chain A residue 76 type BINDING sequence E description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 8) chain A residue 109 type SITE sequence D description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 9) chain A residue 143 type SITE sequence F description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 10) chain A residue 156 type SITE sequence G description Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI4 11) chain A residue 204 type MOD_RES sequence G description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 12) chain A residue 227 type MOD_RES sequence D description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 13) chain A residue 672-684 type prosite sequence EASGTGNMKFMLN description PHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKfmLN source prosite : PS00102 14) chain A residue 378 type catalytic sequence T description 205 source MCSA : MCSA1 15) chain A residue 569 type catalytic sequence R description 205 source MCSA : MCSA1 16) chain A residue 570 type catalytic sequence I description 205 source MCSA : MCSA1 17) chain A residue 575 type catalytic sequence R description 205 source MCSA : MCSA1 18) chain A residue 677 type catalytic sequence G description 205 source MCSA : MCSA1 19) chain A residue 681 type catalytic sequence F description 205 source MCSA : MCSA1 20) chain A residue 15 type MOD_RES sequence V description Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI6 21) chain A residue 430 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 22) chain A residue 473 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9

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