eF-site ID 1z62-A PDB Code 1z62 Chain A click to enlarge Title Indirubin-3'-aminooxy-acetate inhibits glycogen phosphorylase by binding at the inhibitor and the allosteric site. Broad specificities of the two sites Classification TRANSFERASE Compound Glycogen phosphorylase, muscle form Source ORGANISM_COMMON: rabbit; ORGANISM_SCIENTIFIC: Oryctolagus cuniculus; Sequence A:  QISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDY YFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYM GRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGL GNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIC GGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQ GAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPND GGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV VAATLQDIIRRFKSSTNFDAFPDKVAIQLNDTHPSLAIPE LMRVLVDLERLDWDKAWEVTVKTCAYTNHTVLPEALERWP VHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRM SLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIF KDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEIIAERIG EEYISDLDQLRKLLSYVDDEAFIRDVAKVKQENKLKFAAY LEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHVITLYN RIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITAIGD VVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQIST AGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENF FIFGMRVEDVDRLDQRGYNAQEYYDRIPELRQIIEQLSSG FFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVKCQERVS ALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVE PSRQRLPAP Description (1)  Glycogen phosphorylase, muscle form (E.C.2.4.1.1) Functional site 1) chain A residue 134 type sequence G description BINDING SITE FOR RESIDUE PLP A 999 source : AC1 2) chain A residue 491 type sequence W description BINDING SITE FOR RESIDUE PLP A 999 source : AC1 3) chain A residue 568 type sequence K description BINDING SITE FOR RESIDUE PLP A 999 source : AC1 4) chain A residue 574 type sequence K description BINDING SITE FOR RESIDUE PLP A 999 source : AC1 5) chain A residue 648 type sequence Y description BINDING SITE FOR RESIDUE PLP A 999 source : AC1 6) chain A residue 649 type sequence R description BINDING SITE FOR RESIDUE PLP A 999 source : AC1 7) chain A residue 650 type sequence V description BINDING SITE FOR RESIDUE PLP A 999 source : AC1 8) chain A residue 675 type sequence G description BINDING SITE FOR RESIDUE PLP A 999 source : AC1 9) chain A residue 676 type sequence T description BINDING SITE FOR RESIDUE PLP A 999 source : AC1 10) chain A residue 677 type sequence G description BINDING SITE FOR RESIDUE PLP A 999 source : AC1 11) chain A residue 680 type sequence K description BINDING SITE FOR RESIDUE PLP A 999 source : AC1 12) chain A residue 40 type sequence V description BINDING SITE FOR RESIDUE IAA A 990 source : AC2 13) chain A residue 42 type sequence D description BINDING SITE FOR RESIDUE IAA A 990 source : AC2 14) chain A residue 45 type sequence V description BINDING SITE FOR RESIDUE IAA A 990 source : AC2 15) chain A residue 67 type sequence W description BINDING SITE FOR RESIDUE IAA A 990 source : AC2 16) chain A residue 68 type sequence I description BINDING SITE FOR RESIDUE IAA A 990 source : AC2 17) chain A residue 71 type sequence Q description BINDING SITE FOR RESIDUE IAA A 990 source : AC2 18) chain A residue 72 type sequence Q description BINDING SITE FOR RESIDUE IAA A 990 source : AC2 19) chain A residue 193 type sequence R description BINDING SITE FOR RESIDUE IAA A 990 source : AC2 20) chain A residue 309 type sequence R description BINDING SITE FOR RESIDUE IAA A 990 source : AC2 21) chain A residue 310 type sequence R description BINDING SITE FOR RESIDUE IAA A 990 source : AC2 22) chain A residue 45 type sequence V description BINDING SITE FOR RESIDUE IAA A 991 source : AC3 23) chain A residue 196 type sequence F description BINDING SITE FOR RESIDUE IAA A 991 source : AC3 24) chain A residue 242 type sequence R description BINDING SITE FOR RESIDUE IAA A 991 source : AC3 25) chain A residue 309 type sequence R description BINDING SITE FOR RESIDUE IAA A 991 source : AC3 26) chain A residue 282 type sequence N description BINDING SITE FOR RESIDUE IAA A 992 source : AC4 27) chain A residue 285 type sequence F description BINDING SITE FOR RESIDUE IAA A 992 source : AC4 28) chain A residue 382 type sequence E description BINDING SITE FOR RESIDUE IAA A 992 source : AC4 29) chain A residue 572 type sequence E description BINDING SITE FOR RESIDUE IAA A 992 source : AC4 30) chain A residue 610 type sequence A description BINDING SITE FOR RESIDUE IAA A 992 source : AC4 31) chain A residue 612 type sequence G description BINDING SITE FOR RESIDUE IAA A 992 source : AC4 32) chain A residue 613 type sequence Y description BINDING SITE FOR RESIDUE IAA A 992 source : AC4 33) chain A residue 378 type catalytic sequence T description 205 source MCSA : MCSA1 34) chain A residue 569 type catalytic sequence R description 205 source MCSA : MCSA1 35) chain A residue 570 type catalytic sequence I description 205 source MCSA : MCSA1 36) chain A residue 575 type catalytic sequence R description 205 source MCSA : MCSA1 37) chain A residue 677 type catalytic sequence G description 205 source MCSA : MCSA1 38) chain A residue 681 type catalytic sequence F description 205 source MCSA : MCSA1 39) chain A residue 43 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 40) chain A residue 310 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 41) chain A residue 76 type BINDING sequence E description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 42) 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 43) 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 44) 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 45) chain A residue 672-684 type prosite sequence EASGTGNMKFMLN description PHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKfmLN source prosite : PS00102 46) chain A residue 514 type MOD_RES sequence D description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 47) chain A residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 48) chain A residue 748 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 49) 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 50) 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 51) chain A residue 204 type MOD_RES sequence G description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 52) chain A residue 227 type MOD_RES sequence D description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 53) chain A residue 430 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 54) 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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