eF-site ID 2ieg-B PDB Code 2ieg Chain B 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 B:  RKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPR DYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEF YMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDA GLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQK ICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHT GAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPND GYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVV AATLQDIIRRFKSTNFDAFPDKVAIQLNDTHPSLAIPELM RVLVDLERLDWDKAWEVTVKTCAYTNHTVIPEALERWPVH LLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSL VEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKD FYELEPHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEE YISDLDQLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLE REYKVHINPNSLFDVQVKRIHEYKRQLLNCLHVITLYNRI KKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVV NHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAG TEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFI FGMRVEDVDRLDQRGYNAQEYYDRIPELRQIIEQLSSGFF SPKQPDLFKDIVNMLMHHDRFKVFADYEEYVKCQERVSAL YKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPS RQRLP Description (1)  Glycogen phosphorylase, muscle form (E.C.2.4.1.1) Functional site 1) chain B residue 134 type sequence G description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 2) chain B residue 491 type sequence W description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 3) chain B residue 568 type sequence K description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 4) chain B residue 574 type sequence K description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 5) chain B residue 648 type sequence Y description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 6) chain B residue 649 type sequence R description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 7) chain B residue 650 type sequence V description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 8) chain B residue 675 type sequence G description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 9) chain B residue 676 type sequence T description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 10) chain B residue 677 type sequence G description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 11) chain B residue 680 type sequence K description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 12) chain B residue 38 type sequence T description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 13) chain B residue 39 type sequence L description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 14) chain B residue 40 type sequence V description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 15) chain B residue 57 type sequence H description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 16) chain B residue 185 type sequence Y description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 17) chain B residue 186 type sequence G description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 18) chain B residue 60 type sequence R description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 19) chain B residue 188 type sequence P description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 20) chain B residue 190 type sequence E description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 21) chain B residue 191 type sequence K description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 22) chain B residue 192 type sequence A description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 23) chain B residue 378 type catalytic sequence T description 205 source MCSA : MCSA2 24) chain B residue 569 type catalytic sequence R description 205 source MCSA : MCSA2 25) chain B residue 570 type catalytic sequence I description 205 source MCSA : MCSA2 26) chain B residue 575 type catalytic sequence R description 205 source MCSA : MCSA2 27) chain B residue 677 type catalytic sequence G description 205 source MCSA : MCSA2 28) chain B residue 681 type catalytic sequence F description 205 source MCSA : MCSA2 29) chain B residue 43 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 310 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 514 type MOD_RES sequence D description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 32) chain B residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 33) chain B residue 748 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 34) chain B 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 35) chain B residue 76 type BINDING sequence E description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 109 type SITE sequence D description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 37) chain B residue 143 type SITE sequence F description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 38) chain B 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 39) chain B 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 40) chain B residue 204 type MOD_RES sequence G description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 41) chain B residue 227 type MOD_RES sequence D description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 42) chain B residue 430 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 43) chain B residue 473 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9

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