eF-site ID 2ieg-AB PDB Code 2ieg Chain A, 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 A:  QISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDY YFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYM GRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGL GNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIC GGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTQG AKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNGG YIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVA ATLQDIIRRFKSNFDAFPDKVAIQLNDTHPSLAIPELMRV LVDLERLDWDKAWEVTVKTCAYTNHTVIPEALERWPVHLL ETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVE EGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFY ELEPHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYI SDLDQLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLERE YKVHINPNSLFDVQVKRIHEYKRQLLNCLHVITLYNRIKK EPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVVNH DPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTE ASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFG MRVEDVDRLDQRGYNAQEYYDRIPELRQIIEQLSSGFFSP KQPDLFKDIVNMLMHHDRFKVFADYEEYVKCQERVSALYK NPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQ RLP 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 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 B residue 134 type sequence G description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 12) chain B residue 491 type sequence W description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 13) chain B residue 568 type sequence K description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 14) chain B residue 574 type sequence K description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 15) chain B residue 648 type sequence Y description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 16) chain B residue 649 type sequence R description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 17) chain B residue 650 type sequence V description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 18) chain B residue 675 type sequence G description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 19) chain B residue 676 type sequence T description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 20) chain B residue 677 type sequence G description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 21) chain B residue 680 type sequence K description BINDING SITE FOR RESIDUE PLR B 904 source : AC2 22) chain A residue 60 type sequence R description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 23) chain A residue 67 type sequence W description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 24) chain A residue 188 type sequence P description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 25) chain A residue 190 type sequence E description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 26) chain A residue 191 type sequence K description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 27) chain A residue 192 type sequence A description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 28) chain B residue 38 type sequence T description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 29) chain B residue 39 type sequence L description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 30) chain B residue 40 type sequence V description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 31) chain B residue 57 type sequence H description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 32) chain B residue 185 type sequence Y description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 33) chain B residue 186 type sequence G description BINDING SITE FOR RESIDUE FRY A 901 source : AC3 34) chain A residue 38 type sequence T description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 35) chain A residue 39 type sequence L description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 36) chain A residue 40 type sequence V description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 37) chain A residue 53 type sequence F description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 38) chain A residue 57 type sequence H description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 39) chain A residue 185 type sequence Y description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 40) chain A residue 186 type sequence G description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 41) chain B residue 60 type sequence R description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 42) chain B residue 188 type sequence P description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 43) chain B residue 190 type sequence E description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 44) chain B residue 191 type sequence K description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 45) chain B residue 192 type sequence A description BINDING SITE FOR RESIDUE FRY B 902 source : AC4 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 B residue 514 type MOD_RES sequence D description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 50) chain B residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 51) chain B residue 748 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 52) 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 53) 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 54) chain A residue 43 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 55) chain B residue 43 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 56) chain B residue 310 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 57) chain A residue 310 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 58) chain A residue 76 type BINDING sequence E description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 59) chain B residue 76 type BINDING sequence E description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 60) 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 61) 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 62) 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 63) 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 64) 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 65) 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 66) chain A residue 672-684 type prosite sequence EASGTGNMKFMLN description PHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKfmLN source prosite : PS00102 67) chain A residue 378 type catalytic sequence T description 205 source MCSA : MCSA1 68) chain A residue 569 type catalytic sequence R description 205 source MCSA : MCSA1 69) chain A residue 570 type catalytic sequence I description 205 source MCSA : MCSA1 70) chain A residue 575 type catalytic sequence R description 205 source MCSA : MCSA1 71) chain A residue 677 type catalytic sequence G description 205 source MCSA : MCSA1 72) chain A residue 681 type catalytic sequence F description 205 source MCSA : MCSA1 73) chain B residue 378 type catalytic sequence T description 205 source MCSA : MCSA2 74) chain B residue 569 type catalytic sequence R description 205 source MCSA : MCSA2 75) chain B residue 570 type catalytic sequence I description 205 source MCSA : MCSA2 76) chain B residue 575 type catalytic sequence R description 205 source MCSA : MCSA2 77) chain B residue 677 type catalytic sequence G description 205 source MCSA : MCSA2 78) chain B residue 681 type catalytic sequence F description 205 source MCSA : MCSA2 79) 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 80) 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 81) chain A residue 204 type MOD_RES sequence G description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 82) chain B residue 204 type MOD_RES sequence G description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 83) chain B residue 227 type MOD_RES sequence D description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 84) chain A residue 227 type MOD_RES sequence D description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 85) chain A residue 430 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 86) chain B residue 430 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 87) chain A residue 473 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9 88) 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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