eF-site ID 2ieg-A PDB Code 2ieg Chain A click to enlarge Title Crystal structure of rabbit muscle glycogen phosphorylase in complex with 3,4-dihydro-2-quinolone Classification TRANSFERASE Compound Glycogen phosphorylase, muscle form Source ORGANISM_COMMON: rabbit; ORGANISM_SCIENTIFIC: Oryctolagus cuniculus; Sequence A:  QISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDY YFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYM GRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGL GNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIC GGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTQG AKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNGG YIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVA ATLQDIIRRFKSNFDAFPDKVAIQLNDTHPSLAIPELMRV LVDLERLDWDKAWEVTVKTCAYTNHTVIPEALERWPVHLL ETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVE EGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFY ELEPHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYI SDLDQLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLERE YKVHINPNSLFDVQVKRIHEYKRQLLNCLHVITLYNRIKK EPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVVNH DPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTE ASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFG MRVEDVDRLDQRGYNAQEYYDRIPELRQIIEQLSSGFFSP KQPDLFKDIVNMLMHHDRFKVFADYEEYVKCQERVSALYK NPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQ RLP 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 PLR A 903 source : AC1 2) chain A residue 568 type sequence K description BINDING SITE FOR RESIDUE PLR A 903 source : AC1 3) chain A residue 574 type sequence K description BINDING SITE FOR RESIDUE PLR A 903 source : AC1 4) chain A residue 648 type sequence Y description BINDING SITE FOR RESIDUE PLR A 903 source : AC1 5) chain A residue 649 type sequence R description BINDING SITE FOR RESIDUE PLR A 903 source : AC1 6) chain A residue 650 type sequence V description BINDING SITE FOR RESIDUE PLR A 903 source : AC1 7) chain A residue 675 type sequence G description BINDING SITE FOR RESIDUE PLR A 903 source : AC1 8) chain A residue 676 type sequence T description BINDING SITE FOR RESIDUE PLR A 903 source : AC1 9) chain A residue 677 type sequence G description BINDING SITE FOR RESIDUE PLR A 903 source : AC1 10) chain A residue 680 type sequence K description BINDING SITE FOR RESIDUE PLR A 903 source : AC1 11) chain A residue 60 type sequence R description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 12) chain A residue 67 type sequence W description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 13) chain A residue 188 type sequence P description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 14) chain A residue 190 type sequence E description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 15) chain A residue 191 type sequence K description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 16) chain A residue 192 type sequence A description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 17) chain A residue 38 type sequence T description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 18) chain A residue 39 type sequence L description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 19) chain A residue 40 type sequence V description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 20) chain A residue 53 type sequence F description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 21) chain A residue 57 type sequence H description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 22) chain A residue 185 type sequence Y description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 23) chain A residue 186 type sequence G description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 24) chain A residue 514 type MOD_RES sequence D description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 25) chain A residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 26) chain A residue 748 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 27) 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 28) chain A residue 43 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 310 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 76 type BINDING sequence E description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 31) 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 32) 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 33) 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 34) chain A residue 672-684 type prosite sequence EASGTGNMKFMLN description PHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKfmLN source prosite : PS00102 35) chain A residue 378 type catalytic sequence T description 205 source MCSA : MCSA1 36) chain A residue 569 type catalytic sequence R description 205 source MCSA : MCSA1 37) chain A residue 570 type catalytic sequence I description 205 source MCSA : MCSA1 38) chain A residue 575 type catalytic sequence R description 205 source MCSA : MCSA1 39) chain A residue 677 type catalytic sequence G description 205 source MCSA : MCSA1 40) chain A residue 681 type catalytic sequence F description 205 source MCSA : MCSA1 41) 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 42) chain A residue 204 type MOD_RES sequence G description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 43) chain A residue 227 type MOD_RES sequence D description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 44) chain A residue 430 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 45) 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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