eF-site ID 2iei-AB PDB Code 2iei 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 GGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSG AKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPYIQ AVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATL QDIIRRFKSFDAFPDKVAIQLNDTHPSLAIPELMRVLVDL ERLDWDKAWEVTVKTCAYTNHTVIPEALERWPVHLLETLL PRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGAV KRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEP HKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISDLD QLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLEREYVHI NPNSLFDVQVKRIHEYKRQLLNCLHVITLYNRIKKEPNKF VVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVVNHDPVVG DRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGTG NMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVED VDRLDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQPDL FKDIVNMLMHHDRFKVFADYEEYVKCQERVSALYKNPREW TRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSR B:  QISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDY YFALAHTVRDHLVGRWIRTQQHYKDPKRIYYLSLEFYMGR TLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGLGN GGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKICGG WQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQGA KWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPGYIQ AVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATL QDIIRRFKSNFDAFPDKVAIQLNDTHPSLAIPELMRVLVD LERLDWDKAWEVTVKTCAYTNHTVIPEALERWPVHLLETL LPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGA VKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELE PHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISDL DQLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLEREYKH INPNSLFDVQVKRIHEYKRQLLNCLHVITLYNRIKKEPNK FVVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVVNHDPVV GDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGT GNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVE DVDRLDNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKD IVNMLMHHDRFKVFADYEEYVKCQERVSALYKNPREWTRM VIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPA 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 901 source : AC1 2) chain A residue 135 type sequence G description BINDING SITE FOR RESIDUE PLR A 901 source : AC1 3) chain A residue 568 type sequence K description BINDING SITE FOR RESIDUE PLR A 901 source : AC1 4) chain A residue 574 type sequence K description BINDING SITE FOR RESIDUE PLR A 901 source : AC1 5) chain A residue 648 type sequence Y description BINDING SITE FOR RESIDUE PLR A 901 source : AC1 6) chain A residue 649 type sequence R description BINDING SITE FOR RESIDUE PLR A 901 source : AC1 7) chain A residue 650 type sequence V description BINDING SITE FOR RESIDUE PLR A 901 source : AC1 8) chain A residue 675 type sequence G description BINDING SITE FOR RESIDUE PLR A 901 source : AC1 9) chain A residue 676 type sequence T description BINDING SITE FOR RESIDUE PLR A 901 source : AC1 10) chain A residue 677 type sequence G description BINDING SITE FOR RESIDUE PLR A 901 source : AC1 11) chain A residue 680 type sequence K description BINDING SITE FOR RESIDUE PLR A 901 source : AC1 12) chain B residue 90 type sequence Y description BINDING SITE FOR RESIDUE PLR B 902 source : AC2 13) chain B residue 134 type sequence G description BINDING SITE FOR RESIDUE PLR B 902 source : AC2 14) chain B residue 135 type sequence G description BINDING SITE FOR RESIDUE PLR B 902 source : AC2 15) chain B residue 491 type sequence W description BINDING SITE FOR RESIDUE PLR B 902 source : AC2 16) chain B residue 568 type sequence K description BINDING SITE FOR RESIDUE PLR B 902 source : AC2 17) chain B residue 648 type sequence Y description BINDING SITE FOR RESIDUE PLR B 902 source : AC2 18) chain B residue 649 type sequence R description BINDING SITE FOR RESIDUE PLR B 902 source : AC2 19) chain B residue 650 type sequence V description BINDING SITE FOR RESIDUE PLR B 902 source : AC2 20) chain B residue 675 type sequence G description BINDING SITE FOR RESIDUE PLR B 902 source : AC2 21) chain B residue 676 type sequence T description BINDING SITE FOR RESIDUE PLR B 902 source : AC2 22) chain B residue 677 type sequence G description BINDING SITE FOR RESIDUE PLR B 902 source : AC2 23) chain B residue 680 type sequence K description BINDING SITE FOR RESIDUE PLR B 902 source : AC2 24) chain A residue 38 type sequence T description BINDING SITE FOR RESIDUE FRX B 903 source : AC3 25) chain A residue 40 type sequence V description BINDING SITE FOR RESIDUE FRX B 903 source : AC3 26) chain A residue 53 type sequence F description BINDING SITE FOR RESIDUE FRX B 903 source : AC3 27) chain A residue 57 type sequence H description BINDING SITE FOR RESIDUE FRX B 903 source : AC3 28) chain A residue 60 type sequence R description BINDING SITE FOR RESIDUE FRX B 903 source : AC3 29) chain A residue 185 type sequence Y description BINDING SITE FOR RESIDUE FRX B 903 source : AC3 30) chain B residue 60 type sequence R description BINDING SITE FOR RESIDUE FRX B 903 source : AC3 31) chain B residue 67 type sequence W description BINDING SITE FOR RESIDUE FRX B 903 source : AC3 32) chain B residue 190 type sequence E description BINDING SITE FOR RESIDUE FRX B 903 source : AC3 33) chain B residue 191 type sequence K description BINDING SITE FOR RESIDUE FRX B 903 source : AC3 34) chain A residue 60 type sequence R description BINDING SITE FOR RESIDUE FRX A 904 source : AC4 35) chain A residue 188 type sequence P description BINDING SITE FOR RESIDUE FRX A 904 source : AC4 36) chain A residue 190 type sequence E description BINDING SITE FOR RESIDUE FRX A 904 source : AC4 37) chain A residue 191 type sequence K description BINDING SITE FOR RESIDUE FRX A 904 source : AC4 38) chain A residue 192 type sequence A description BINDING SITE FOR RESIDUE FRX A 904 source : AC4 39) chain B residue 38 type sequence T description BINDING SITE FOR RESIDUE FRX A 904 source : AC4 40) chain B residue 39 type sequence L description BINDING SITE FOR RESIDUE FRX A 904 source : AC4 41) chain B residue 40 type sequence V description BINDING SITE FOR RESIDUE FRX A 904 source : AC4 42) chain B residue 57 type sequence H description BINDING SITE FOR RESIDUE FRX A 904 source : AC4 43) chain B residue 184 type sequence R description BINDING SITE FOR RESIDUE FRX A 904 source : AC4 44) chain B residue 185 type sequence Y description BINDING SITE FOR RESIDUE FRX A 904 source : AC4 45) chain A residue 378 type catalytic sequence T description 205 source MCSA : MCSA1 46) chain A residue 569 type catalytic sequence R description 205 source MCSA : MCSA1 47) chain A residue 570 type catalytic sequence I description 205 source MCSA : MCSA1 48) chain A residue 575 type catalytic sequence R description 205 source MCSA : MCSA1 49) chain A residue 677 type catalytic sequence G description 205 source MCSA : MCSA1 50) chain A residue 681 type catalytic sequence F description 205 source MCSA : MCSA1 51) chain B residue 378 type catalytic sequence T description 205 source MCSA : MCSA2 52) chain B residue 569 type catalytic sequence R description 205 source MCSA : MCSA2 53) chain B residue 570 type catalytic sequence I description 205 source MCSA : MCSA2 54) chain B residue 575 type catalytic sequence R description 205 source MCSA : MCSA2 55) chain B residue 677 type catalytic sequence G description 205 source MCSA : MCSA2 56) chain B residue 681 type catalytic sequence F description 205 source MCSA : MCSA2 57) chain A residue 672-684 type prosite sequence EASGTGNMKFMLN description PHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKfmLN source prosite : PS00102 58) chain A residue 43 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 59) chain A residue 310 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 60) chain B residue 43 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 61) chain B residue 310 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 62) chain A residue 514 type MOD_RES sequence D description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 63) chain A residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 64) chain A residue 748 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 65) chain B residue 514 type MOD_RES sequence D description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 66) chain B residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 67) chain B residue 748 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 68) 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 69) 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 70) chain A residue 76 type BINDING sequence E description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 71) 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 72) 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 73) 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 74) 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 75) 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 76) 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 77) 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 78) 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 79) chain A residue 204 type MOD_RES sequence G description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 80) chain A residue 227 type MOD_RES sequence D description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 81) chain B residue 204 type MOD_RES sequence G description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 82) chain B residue 227 type MOD_RES sequence D description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 83) chain A residue 430 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 84) chain B residue 430 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 85) chain A residue 473 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9 86) chain B residue 473 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9

Display surface Download Links