eF-site ID 3e3n-H PDB Code 3e3n Chain H click to enlarge 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 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 H residue 42 type sequence D description BINDING SITE FOR RESIDUE AMP G 843 source : CC1 2) chain H residue 44 type sequence N description BINDING SITE FOR RESIDUE AMP G 843 source : CC1 3) chain H residue 43 type sequence R description BINDING SITE FOR RESIDUE SO4 G 844 source : CC2 4) chain H residue 67 type sequence W description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 5) chain H residue 71 type sequence Q description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 6) chain H residue 75 type sequence Y description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 7) chain H residue 309 type sequence R description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 8) chain H residue 310 type sequence R description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 9) chain H residue 315 type sequence K description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 10) chain H residue 316 type sequence F description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 11) chain H residue 317 type sequence G description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 12) chain H residue 318 type sequence C description BINDING SITE FOR RESIDUE AMP H 843 source : CC4 13) chain H residue 11 type sequence K description BINDING SITE FOR RESIDUE SO4 H 844 source : CC5 14) chain H residue 14 type sequence S description BINDING SITE FOR RESIDUE SO4 H 844 source : CC5 15) chain H residue 69 type sequence R description BINDING SITE FOR RESIDUE SO4 H 844 source : CC5 16) chain H residue 133 type sequence N description BINDING SITE FOR RESIDUE SO4 H 899 source : CC6 17) chain H residue 135 type sequence G description BINDING SITE FOR RESIDUE SO4 H 899 source : CC6 18) chain H residue 569 type sequence R description BINDING SITE FOR RESIDUE SO4 H 899 source : CC6 19) chain H residue 513 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 20) chain H residue 746 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 21) chain H residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 22) 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 23) chain H residue 42 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 24) chain H residue 309 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 25) chain H residue 75 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 26) 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 27) 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 28) 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 29) 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 30) chain H residue 203 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 31) chain H residue 226 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 32) chain H residue 429 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 33) chain H residue 472 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9 34) chain H residue 377 type catalytic sequence H description 205 source MCSA : MCSA8 35) chain H residue 568 type catalytic sequence K description 205 source MCSA : MCSA8 36) chain H residue 569 type catalytic sequence R description 205 source MCSA : MCSA8 37) chain H residue 574 type catalytic sequence K description 205 source MCSA : MCSA8 38) chain H residue 676 type catalytic sequence T description 205 source MCSA : MCSA8 39) chain H residue 680 type catalytic sequence X description 205 source MCSA : MCSA8

Display surface Download Links