eF-site ID 3e3n-ABCDEFGH PDB Code 3e3n Chain A, B, C, D, E, F, G, H Title The Glycogen phosphorylase b R state- AMP complex Classification TRANSFERASE Compound Glycogen phosphorylase, muscle form Source ORGANISM_COMMON: European rabbit,Japanese white rabbit,domestic rabbit,rabbits; ORGANISM_SCIENTIFIC: Oryctolagus cuniculus; Sequence A:  QEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVA TPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLS LEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIE EDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIF NQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRV EHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSA KAPNGYIQAVLDRNLAENISRVLYGKELRLKQEYFVVAAT LQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPS LAIPELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVLPEA LERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVD RLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEIL KKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEII AERIGEEYISDLDQLRKLLSYVDDEAFIRDVAKVKQENKL KFAAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHV ITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLI TAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLS EQISTAGTEASGTGNMXFMLNGALTIGTMDGANVEMAEEA GEENFFIFGMRVEDVDRLDQRGYNAQEYYDRIPELRQIIE QLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVKC QERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYARE IWGVEPSRQRLPAP B:  QEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVA TPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLS LEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIE EDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIF NQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRV EHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSA KAPNGYIQAVLDRNLAENISRVLYPGKELRLKQEYFVVAA TLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHP SLAIPELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVLPE ALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDV DRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEI LKKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEI IAERIGEEYISDLDQLRKLLSYVDDEAFIRDVAKVKQENK LKFAAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLH VITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKL ITAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADL SEQISTAGTEASGTGNMXFMLNGALTIGTMDGANVEMAEE AGEENFFIFGMRVEDVDRLDQRGYNAQEYYDRIPELRQII EQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVK CQERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAR EIWGVEPSRQRLPAP C:  KRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATP RDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLE FYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEED AGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQ KICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEH TSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKA PNGYIQAVLDRNLAENISRVLYGKELRLKQEYFVVAATLQ DIIRRFKSSNFDAFPDKVAIQLNDTHPSLAIPELMRVLVD LERLDWDKAWEVTVKTCAYTNHTVLPEALERWPVHLLETL LPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGA VKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELE PHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISDL DQLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLEREYKV HINPNSLFDVQVKRIHEYKRQLLNCLHVITLYNRIKKEPN KFVVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVVNHDPV VGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASG TGNMXFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRV EDVDRLDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQP DLFKDIVNMLMHHDRFKVFADYEEYVKCQERVSALYKNPR EWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLP AP D:  QEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVA TPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLS LEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIE EDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIF NQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRV EHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSA KAPNGYIQAVLDRNLAENISRVLYGKELRLKQEYFVVAAT LQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPS LAIPELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVLPEA LERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVD RLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEIL KKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEII AERIGEEYISDLDQLRKLLSYVDDEAFIRDVAKVKQENKL KFAAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHV ITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLI TAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLS EQISTAGTEASGTGNMXFMLNGALTIGTMDGANVEMAEEA GEENFFIFGMRVEDVDRLDQRGYNAQEYYDRIPELRQIIE QLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVKC QERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYARE IWGVEPSRQRLPAPD E:  EKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVAT PRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSL EFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEE DAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFN QKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVE HTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAK APNGYIQAVLDRNLAENISRVLYGKELRLKQEYFVVAATL QDIIRRFKSSNFDAFPDKVAIQLNDTHPSLAIPELMRVLV DLERLDWDKAWEVTVKTCAYTNHTVLPEALERWPVHLLET LLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEG AVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYEL EPHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISD LDQLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLEREYK VHINPNSLFDVQVKRIHEYKRQLLNCLHVITLYNRIKKEP NKFVVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVVNHDP VVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEAS GTGNMXFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMR VEDVDRLDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQ PDLFKDIVNMLMHHDRFKVFADYEEYVKCQERVSALYKNP REWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRL PAP F:  EKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVAT PRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSL EFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEE DAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFN QKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVE HTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAK APNGYIQAVLDRNLAENISRVLYGKELRLKQEYFVVAATL QDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSL AIPELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVLPEAL ERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDR LRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILK KTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEIIA ERIGEEYISDLDQLRKLLSYVDDEAFIRDVAKVKQENKLK FAAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHVI TLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLIT AIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSE QISTAGTEASGTGNMXFMLNGALTIGTMDGANVEMAEEAG EENFFIFGMRVEDVDRLDQRGYNAQEYYDRIPELRQIIEQ LSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVKCQ ERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREI WGVEPSRQRLPAP G:  QEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVA TPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLS LEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIE EDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIF NQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRV EHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSA KAPNGYIQAVLDRNLAENISRVLYGKELRLKQEYFVVAAT LQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPS LAIPELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVLPEA LERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVD RLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEIL KKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEII AERIGEEYISDLDQLRKLLSYVDDEAFIRDVAKVKQENKL KFAAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHV ITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLI TAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLS EQISTAGTEASGTGNMXFMLNGALTIGTMDGANVEMAEEA GEENFFIFGMRVEDVDRLDQRGYNAQEYYDRIPELRQIIE QLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVKC QERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYARE IWGVEPSRQRLPAP H:  DQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNV ATPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYL SLEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEI EEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGI FNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGR VEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWS AKAPNGYIQAVLDRNLAENISRVLYGKELRLKQEYFVVAA TLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHP SLAIPELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVLPE ALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDV DRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEI LKKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEI IAERIGEEYISDLDQLRKLLSYVDDEAFIRDVAKVKQENK LKFAAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLH VITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKL ITAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADL SEQISTAGTEASGTGNMXFMLNGALTIGTMDGANVEMAEE AGEENFFIFGMRVEDVDRLDQRGYNAQEYYDRIPELRQII EQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVK CQERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAR EIWGVEPSRQRLPA Description Functional site 1) chain A residue 67 type sequence W description BINDING SITE FOR RESIDUE AMP A 843 source : AC1 2) chain A residue 71 type sequence Q description BINDING SITE FOR RESIDUE AMP A 843 source : AC1 3) chain A residue 75 type sequence Y description BINDING SITE FOR RESIDUE AMP A 843 source : AC1 4) chain A residue 309 type sequence R description BINDING SITE FOR RESIDUE AMP A 843 source : AC1 5) chain A residue 310 type sequence R description BINDING SITE FOR RESIDUE AMP A 843 source : AC1 6) chain A residue 315 type sequence K description BINDING SITE FOR RESIDUE AMP A 843 source : AC1 7) chain A residue 316 type sequence F description BINDING SITE FOR RESIDUE AMP A 843 source : AC1 8) chain A residue 317 type sequence G description BINDING SITE FOR RESIDUE AMP A 843 source : AC1 9) chain A residue 318 type sequence C description BINDING SITE FOR RESIDUE AMP A 843 source : AC1 10) chain B residue 42 type sequence D description BINDING SITE FOR RESIDUE AMP A 843 source : AC1 11) chain B residue 44 type sequence N description BINDING SITE FOR RESIDUE AMP A 843 source : AC1 12) chain B residue 45 type sequence V description BINDING SITE FOR RESIDUE AMP A 843 source : AC1 13) chain A residue 14 type sequence S description BINDING SITE FOR RESIDUE SO4 A 844 source : AC2 14) chain A residue 16 type sequence R description BINDING SITE FOR RESIDUE SO4 A 844 source : AC2 15) chain A residue 69 type sequence R description BINDING SITE FOR RESIDUE SO4 A 844 source : AC2 16) chain B residue 43 type sequence R description BINDING SITE FOR RESIDUE SO4 A 844 source : AC2 17) chain A residue 135 type sequence G description BINDING SITE FOR RESIDUE SO4 A 845 source : AC3 18) chain A residue 569 type sequence R description BINDING SITE FOR RESIDUE SO4 A 845 source : AC3 19) chain A residue 574 type sequence K description BINDING SITE FOR RESIDUE SO4 A 845 source : AC3 20) chain A residue 42 type sequence D description BINDING SITE FOR RESIDUE AMP B 843 source : AC4 21) chain A residue 44 type sequence N description BINDING SITE FOR RESIDUE AMP B 843 source : AC4 22) chain A residue 45 type sequence V description BINDING SITE FOR RESIDUE AMP B 843 source : AC4 23) chain B residue 67 type sequence W description BINDING SITE FOR RESIDUE AMP B 843 source : AC4 24) chain B residue 71 type sequence Q description BINDING SITE FOR RESIDUE AMP B 843 source : AC4 25) chain B residue 75 type sequence Y description BINDING SITE FOR RESIDUE AMP B 843 source : AC4 26) chain B residue 309 type sequence R description BINDING SITE FOR RESIDUE AMP B 843 source : AC4 27) chain B residue 310 type sequence R description BINDING SITE FOR RESIDUE AMP B 843 source : AC4 28) chain B residue 315 type sequence K description BINDING SITE FOR RESIDUE AMP B 843 source : AC4 29) chain B residue 316 type sequence F description BINDING SITE FOR RESIDUE AMP B 843 source : AC4 30) chain B residue 317 type sequence G description BINDING SITE FOR RESIDUE AMP B 843 source : AC4 31) chain B residue 318 type sequence C description BINDING SITE FOR RESIDUE AMP B 843 source : AC4 32) chain A residue 43 type sequence R description BINDING SITE FOR RESIDUE SO4 B 844 source : AC5 33) chain B residue 14 type sequence S description BINDING SITE FOR RESIDUE SO4 B 844 source : AC5 34) chain B residue 16 type sequence R description BINDING SITE FOR RESIDUE SO4 B 844 source : AC5 35) chain B residue 69 type sequence R description BINDING SITE FOR RESIDUE SO4 B 844 source : AC5 36) chain B residue 134 type sequence G description BINDING SITE FOR RESIDUE SO4 B 845 source : AC6 37) chain B residue 135 type sequence G description BINDING SITE FOR RESIDUE SO4 B 845 source : AC6 38) chain B residue 569 type sequence R description BINDING SITE FOR RESIDUE SO4 B 845 source : AC6 39) chain B residue 574 type sequence K description BINDING SITE FOR RESIDUE SO4 B 845 source : AC6 40) chain C residue 67 type sequence W description BINDING SITE FOR RESIDUE AMP C 843 source : AC7 41) chain C residue 71 type sequence Q description BINDING SITE FOR RESIDUE AMP C 843 source : AC7 42) chain C residue 75 type sequence Y description BINDING SITE FOR RESIDUE AMP C 843 source : AC7 43) chain C residue 309 type sequence R description BINDING SITE FOR RESIDUE AMP C 843 source : AC7 44) chain C residue 310 type sequence R description BINDING SITE FOR RESIDUE AMP C 843 source : AC7 45) chain D residue 42 type sequence D description BINDING SITE FOR RESIDUE AMP C 843 source : AC7 46) chain D residue 44 type sequence N description BINDING SITE FOR RESIDUE AMP C 843 source : AC7 47) chain D residue 45 type sequence V description BINDING SITE FOR RESIDUE AMP C 843 source : AC7 48) chain C residue 135 type sequence G description BINDING SITE FOR RESIDUE SO4 C 844 source : AC8 49) chain C residue 569 type sequence R description BINDING SITE FOR RESIDUE SO4 C 844 source : AC8 50) chain C residue 574 type sequence K description BINDING SITE FOR RESIDUE SO4 C 844 source : AC8 51) chain C residue 680 type sequence X description BINDING SITE FOR RESIDUE SO4 C 844 source : AC8 52) chain C residue 43 type sequence R description BINDING SITE FOR RESIDUE SO4 C 845 source : AC9 53) chain D residue 14 type sequence S description BINDING SITE FOR RESIDUE SO4 C 845 source : AC9 54) chain D residue 16 type sequence R description BINDING SITE FOR RESIDUE SO4 C 845 source : AC9 55) chain D residue 69 type sequence R description BINDING SITE FOR RESIDUE SO4 C 845 source : AC9 56) chain C residue 42 type sequence D description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 57) chain C residue 44 type sequence N description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 58) chain C residue 45 type sequence V description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 59) chain D residue 67 type sequence W description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 60) chain D residue 71 type sequence Q description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 61) chain D residue 75 type sequence Y description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 62) chain D residue 309 type sequence R description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 63) chain D residue 310 type sequence R description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 64) chain D residue 315 type sequence K description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 65) chain D residue 317 type sequence G description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 66) chain D residue 318 type sequence C description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 67) chain C residue 14 type sequence S description BINDING SITE FOR RESIDUE SO4 D 844 source : BC2 68) chain C residue 16 type sequence R description BINDING SITE FOR RESIDUE SO4 D 844 source : BC2 69) chain C residue 69 type sequence R description BINDING SITE FOR RESIDUE SO4 D 844 source : BC2 70) chain D residue 43 type sequence R description BINDING SITE FOR RESIDUE SO4 D 844 source : BC2 71) chain D residue 135 type sequence G description BINDING SITE FOR RESIDUE SO4 D 845 source : BC3 72) chain D residue 569 type sequence R description BINDING SITE FOR RESIDUE SO4 D 845 source : BC3 73) chain D residue 574 type sequence K description BINDING SITE FOR RESIDUE SO4 D 845 source : BC3 74) chain D residue 680 type sequence X description BINDING SITE FOR RESIDUE SO4 D 845 source : BC3 75) chain E residue 67 type sequence W description BINDING SITE FOR RESIDUE AMP E 843 source : BC4 76) chain E residue 71 type sequence Q description BINDING SITE FOR RESIDUE AMP E 843 source : BC4 77) chain E residue 75 type sequence Y description BINDING SITE FOR RESIDUE AMP E 843 source : BC4 78) chain E residue 309 type sequence R description BINDING SITE FOR RESIDUE AMP E 843 source : BC4 79) chain E residue 310 type sequence R description BINDING SITE FOR RESIDUE AMP E 843 source : BC4 80) chain F residue 42 type sequence D description BINDING SITE FOR RESIDUE AMP E 843 source : BC4 81) chain F residue 44 type sequence N description BINDING SITE FOR RESIDUE AMP E 843 source : BC4 82) chain F residue 45 type sequence V description BINDING SITE FOR RESIDUE AMP E 843 source : BC4 83) chain E residue 14 type sequence S description BINDING SITE FOR RESIDUE SO4 E 844 source : BC5 84) chain E residue 16 type sequence R description BINDING SITE FOR RESIDUE SO4 E 844 source : BC5 85) chain E residue 69 type sequence R description BINDING SITE FOR RESIDUE SO4 E 844 source : BC5 86) chain F residue 43 type sequence R description BINDING SITE FOR RESIDUE SO4 E 844 source : BC5 87) chain E residue 135 type sequence G description BINDING SITE FOR RESIDUE SO4 E 845 source : BC6 88) chain E residue 569 type sequence R description BINDING SITE FOR RESIDUE SO4 E 845 source : BC6 89) chain E residue 680 type sequence X description BINDING SITE FOR RESIDUE SO4 E 845 source : BC6 90) chain E residue 42 type sequence D description BINDING SITE FOR RESIDUE AMP F 843 source : BC7 91) chain E residue 44 type sequence N description BINDING SITE FOR RESIDUE AMP F 843 source : BC7 92) chain E residue 45 type sequence V description BINDING SITE FOR RESIDUE AMP F 843 source : BC7 93) chain F residue 71 type sequence Q description BINDING SITE FOR RESIDUE AMP F 843 source : BC7 94) chain F residue 75 type sequence Y description BINDING SITE FOR RESIDUE AMP F 843 source : BC7 95) chain F residue 309 type sequence R description BINDING SITE FOR RESIDUE AMP F 843 source : BC7 96) chain F residue 310 type sequence R description BINDING SITE FOR RESIDUE AMP F 843 source : BC7 97) chain F residue 315 type sequence K description BINDING SITE FOR RESIDUE AMP F 843 source : BC7 98) chain F residue 316 type sequence F description BINDING SITE FOR RESIDUE AMP F 843 source : BC7 99) chain F residue 317 type sequence G description BINDING SITE FOR RESIDUE AMP F 843 source : BC7 100) chain F residue 318 type sequence C description BINDING SITE FOR RESIDUE AMP F 843 source : BC7 101) chain E residue 43 type sequence R description BINDING SITE FOR RESIDUE SO4 F 844 source : BC8 102) chain F residue 11 type sequence K description BINDING SITE FOR RESIDUE SO4 F 844 source : BC8 103) chain F residue 14 type sequence S description BINDING SITE FOR RESIDUE SO4 F 844 source : BC8 104) chain F residue 16 type sequence R description BINDING SITE FOR RESIDUE SO4 F 844 source : BC8 105) chain F residue 69 type sequence R description BINDING SITE FOR RESIDUE SO4 F 844 source : BC8 106) chain F residue 135 type sequence G description BINDING SITE FOR RESIDUE SO4 F 845 source : BC9 107) chain F residue 569 type sequence R description BINDING SITE FOR RESIDUE SO4 F 845 source : BC9 108) chain F residue 574 type sequence K description BINDING SITE FOR RESIDUE SO4 F 845 source : BC9 109) chain F residue 680 type sequence X description BINDING SITE FOR RESIDUE SO4 F 845 source : BC9 110) chain G residue 67 type sequence W description BINDING SITE FOR RESIDUE AMP G 843 source : CC1 111) chain G residue 71 type sequence Q description BINDING SITE FOR RESIDUE AMP G 843 source : CC1 112) chain G residue 75 type sequence Y description BINDING SITE FOR RESIDUE AMP G 843 source : CC1 113) chain G residue 309 type sequence R description BINDING SITE FOR RESIDUE AMP G 843 source : CC1 114) chain G residue 310 type sequence R description BINDING SITE FOR RESIDUE AMP G 843 source : CC1 115) chain G residue 315 type sequence K description BINDING SITE FOR RESIDUE AMP G 843 source : CC1 116) chain G residue 316 type sequence F description BINDING SITE FOR RESIDUE AMP G 843 source : CC1 117) chain G residue 317 type sequence G description BINDING SITE FOR RESIDUE AMP G 843 source : CC1 118) chain G residue 318 type sequence C description BINDING SITE FOR RESIDUE AMP G 843 source : CC1 119) chain H residue 42 type sequence D description BINDING SITE FOR RESIDUE AMP G 843 source : CC1 120) chain H residue 44 type sequence N description BINDING SITE FOR RESIDUE AMP G 843 source : CC1 121) chain G residue 14 type sequence S description BINDING SITE FOR RESIDUE SO4 G 844 source : CC2 122) chain G residue 16 type sequence R description BINDING SITE FOR RESIDUE SO4 G 844 source : CC2 123) chain G residue 69 type sequence R description BINDING SITE FOR RESIDUE SO4 G 844 source : CC2 124) chain H residue 43 type sequence R description BINDING SITE FOR RESIDUE SO4 G 844 source : CC2 125) chain G residue 135 type sequence G description BINDING SITE FOR RESIDUE SO4 G 845 source : CC3 126) chain G residue 569 type sequence R description BINDING SITE FOR RESIDUE SO4 G 845 source : CC3 127) chain G residue 574 type sequence K description BINDING SITE FOR RESIDUE SO4 G 845 source : CC3 128) chain G residue 680 type sequence X description BINDING SITE FOR RESIDUE SO4 G 845 source : CC3 129) chain G residue 42 type sequence D description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 130) chain G residue 44 type sequence N description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 131) chain G residue 45 type sequence V description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 132) chain H residue 67 type sequence W description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 133) chain H residue 71 type sequence Q description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 134) chain H residue 75 type sequence Y description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 135) chain H residue 309 type sequence R description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 136) chain H residue 310 type sequence R description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 137) chain H residue 315 type sequence K description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 138) chain H residue 316 type sequence F description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 139) chain H residue 317 type sequence G description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 140) chain H residue 318 type sequence C description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 141) chain G residue 43 type sequence R description BINDING SITE FOR RESIDUE SO4 H 844 source : CC5 142) chain H residue 11 type sequence K description BINDING SITE FOR RESIDUE SO4 H 844 source : CC5 143) chain H residue 14 type sequence S description BINDING SITE FOR RESIDUE SO4 H 844 source : CC5 144) chain H residue 69 type sequence R description BINDING SITE FOR RESIDUE SO4 H 844 source : CC5 145) chain H residue 133 type sequence N description BINDING SITE FOR RESIDUE SO4 H 899 source : CC6 146) chain H residue 135 type sequence G description BINDING SITE FOR RESIDUE SO4 H 899 source : CC6 147) chain H residue 569 type sequence R description BINDING SITE FOR RESIDUE SO4 H 899 source : CC6 148) chain A residue 513 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 149) chain A residue 746 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 150) chain A residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 151) chain B residue 513 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 152) chain B residue 746 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 153) chain C residue 746 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 154) chain D residue 513 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 155) chain D residue 746 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 156) chain D residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 157) chain E residue 513 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 158) chain E residue 746 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 159) chain E residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 160) chain F residue 513 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 161) chain F residue 746 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 162) chain F residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 163) chain G residue 513 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 164) chain G residue 746 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 165) chain G residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 166) chain H residue 513 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 167) chain H residue 746 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 168) chain H residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 169) chain C residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 170) chain B residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 171) chain C residue 513 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 172) chain A residue 680 type MOD_RES sequence X 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 173) chain B residue 680 type MOD_RES sequence X 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 174) chain C residue 680 type MOD_RES sequence X 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 175) chain D residue 680 type MOD_RES sequence X 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 176) chain E residue 680 type MOD_RES sequence X 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 177) chain F residue 680 type MOD_RES sequence X 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 178) chain G residue 680 type MOD_RES sequence X 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 179) chain H residue 680 type MOD_RES sequence X 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 180) chain A residue 42 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 181) chain A residue 309 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 182) chain E residue 309 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 183) chain F residue 42 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 184) chain F residue 309 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 185) chain G residue 42 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 186) chain G residue 309 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 187) chain H residue 42 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 188) chain H residue 309 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 189) chain E residue 42 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 190) chain B residue 42 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 191) chain B residue 309 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 192) chain C residue 42 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 193) chain C residue 309 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 194) chain D residue 42 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 195) chain D residue 309 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 196) chain B residue 75 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 197) chain C residue 75 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 198) chain D residue 75 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 199) chain E residue 75 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 200) chain F residue 75 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 201) chain G residue 75 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 202) chain H residue 75 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 203) chain A residue 75 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 204) chain A residue 108 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 205) chain A residue 142 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 206) chain E residue 142 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 207) chain F residue 108 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 208) chain F residue 142 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 209) chain G residue 108 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 210) chain G residue 142 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 211) chain H residue 108 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 212) chain H residue 142 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 213) chain E residue 108 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 214) chain B residue 108 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 215) chain B residue 142 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 216) chain C residue 108 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 217) chain C residue 142 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 218) chain D residue 108 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 219) chain D residue 142 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 220) chain A residue 155 type SITE sequence Y description Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI4 221) chain B residue 155 type SITE sequence Y description Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI4 222) chain C residue 155 type SITE sequence Y description Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI4 223) chain D residue 155 type SITE sequence Y description Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI4 224) chain E residue 155 type SITE sequence Y description Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI4 225) chain F residue 155 type SITE sequence Y description Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI4 226) chain G residue 155 type SITE sequence Y description Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI4 227) chain H residue 155 type SITE sequence Y description Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI4 228) chain A residue 14 type MOD_RES sequence S description Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI6 229) chain B residue 14 type MOD_RES sequence S description Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI6 230) chain C residue 14 type MOD_RES sequence S description Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI6 231) chain D residue 14 type MOD_RES sequence S description Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI6 232) chain E residue 14 type MOD_RES sequence S description Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI6 233) chain F residue 14 type MOD_RES sequence S description Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI6 234) chain G residue 14 type MOD_RES sequence S description Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI6 235) chain H residue 14 type MOD_RES sequence S description Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI6 236) chain A residue 203 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 237) chain E residue 226 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 238) chain F residue 203 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 239) chain F residue 226 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 240) chain G residue 203 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 241) chain G residue 226 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 242) chain H residue 203 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 243) chain H residue 226 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 244) chain E residue 203 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 245) chain A residue 226 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 246) chain B residue 203 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 247) chain B residue 226 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 248) chain C residue 203 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 249) chain C residue 226 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 250) chain D residue 203 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 251) chain D residue 226 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 252) chain A residue 429 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 253) chain B residue 429 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 254) chain C residue 429 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 255) chain D residue 429 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 256) chain E residue 429 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 257) chain F residue 429 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 258) chain G residue 429 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 259) chain H residue 429 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 260) chain A residue 472 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9 261) chain H residue 472 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9 262) chain B residue 472 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9 263) chain C residue 472 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9 264) chain D residue 472 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9 265) chain E residue 472 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9 266) chain F residue 472 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9 267) chain G residue 472 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9 268) chain A residue 672-684 type prosite sequence EASGTGNMXFMLN description PHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKfmLN source prosite : PS00102 269) chain A residue 377 type catalytic sequence H description 205 source MCSA : MCSA1 270) chain A residue 568 type catalytic sequence K description 205 source MCSA : MCSA1 271) chain A residue 569 type catalytic sequence R description 205 source MCSA : MCSA1 272) chain A residue 574 type catalytic sequence K description 205 source MCSA : MCSA1 273) chain A residue 676 type catalytic sequence T description 205 source MCSA : MCSA1 274) chain A residue 680 type catalytic sequence X description 205 source MCSA : MCSA1 275) chain B residue 377 type catalytic sequence H description 205 source MCSA : MCSA2 276) chain B residue 568 type catalytic sequence K description 205 source MCSA : MCSA2 277) chain B residue 569 type catalytic sequence R description 205 source MCSA : MCSA2 278) chain B residue 574 type catalytic sequence K description 205 source MCSA : MCSA2 279) chain B residue 676 type catalytic sequence T description 205 source MCSA : MCSA2 280) chain B residue 680 type catalytic sequence X description 205 source MCSA : MCSA2 281) chain C residue 377 type catalytic sequence H description 205 source MCSA : MCSA3 282) chain C residue 568 type catalytic sequence K description 205 source MCSA : MCSA3 283) chain C residue 569 type catalytic sequence R description 205 source MCSA : MCSA3 284) chain C residue 574 type catalytic sequence K description 205 source MCSA : MCSA3 285) chain C residue 676 type catalytic sequence T description 205 source MCSA : MCSA3 286) chain C residue 680 type catalytic sequence X description 205 source MCSA : MCSA3 287) chain D residue 377 type catalytic sequence H description 205 source MCSA : MCSA4 288) chain D residue 568 type catalytic sequence K description 205 source MCSA : MCSA4 289) chain D residue 569 type catalytic sequence R description 205 source MCSA : MCSA4 290) chain D residue 574 type catalytic sequence K description 205 source MCSA : MCSA4 291) chain D residue 676 type catalytic sequence T description 205 source MCSA : MCSA4 292) chain D residue 680 type catalytic sequence X description 205 source MCSA : MCSA4 293) chain E residue 377 type catalytic sequence H description 205 source MCSA : MCSA5 294) chain E residue 568 type catalytic sequence K description 205 source MCSA : MCSA5 295) chain E residue 569 type catalytic sequence R description 205 source MCSA : MCSA5 296) chain E residue 574 type catalytic sequence K description 205 source MCSA : MCSA5 297) chain E residue 676 type catalytic sequence T description 205 source MCSA : MCSA5 298) chain E residue 680 type catalytic sequence X description 205 source MCSA : MCSA5 299) chain F residue 377 type catalytic sequence H description 205 source MCSA : MCSA6 300) chain F residue 568 type catalytic sequence K description 205 source MCSA : MCSA6 301) chain F residue 569 type catalytic sequence R description 205 source MCSA : MCSA6 302) chain F residue 574 type catalytic sequence K description 205 source MCSA : MCSA6 303) chain F residue 676 type catalytic sequence T description 205 source MCSA : MCSA6 304) chain F residue 680 type catalytic sequence X description 205 source MCSA : MCSA6 305) chain G residue 377 type catalytic sequence H description 205 source MCSA : MCSA7 306) chain G residue 568 type catalytic sequence K description 205 source MCSA : MCSA7 307) chain G residue 569 type catalytic sequence R description 205 source MCSA : MCSA7 308) chain G residue 574 type catalytic sequence K description 205 source MCSA : MCSA7 309) chain G residue 676 type catalytic sequence T description 205 source MCSA : MCSA7 310) chain G residue 680 type catalytic sequence X description 205 source MCSA : MCSA7 311) chain H residue 377 type catalytic sequence H description 205 source MCSA : MCSA8 312) chain H residue 568 type catalytic sequence K description 205 source MCSA : MCSA8 313) chain H residue 569 type catalytic sequence R description 205 source MCSA : MCSA8 314) chain H residue 574 type catalytic sequence K description 205 source MCSA : MCSA8 315) chain H residue 676 type catalytic sequence T description 205 source MCSA : MCSA8 316) chain H residue 680 type catalytic sequence X description 205 source MCSA : MCSA8

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