eF-site ID 3e3n-D PDB Code 3e3n Chain D 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 D:  QEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVA TPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLS LEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIE EDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIF NQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRV EHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSA KAPNGYIQAVLDRNLAENISRVLYGKELRLKQEYFVVAAT LQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPS LAIPELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVLPEA LERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVD RLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEIL KKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEII AERIGEEYISDLDQLRKLLSYVDDEAFIRDVAKVKQENKL KFAAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHV ITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLI TAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLS EQISTAGTEASGTGNMXFMLNGALTIGTMDGANVEMAEEA GEENFFIFGMRVEDVDRLDQRGYNAQEYYDRIPELRQIIE QLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVKC QERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYARE IWGVEPSRQRLPAPD Description Functional site 1) chain D residue 42 type sequence D description BINDING SITE FOR RESIDUE AMP C 843 source : AC7 2) chain D residue 44 type sequence N description BINDING SITE FOR RESIDUE AMP C 843 source : AC7 3) chain D residue 45 type sequence V description BINDING SITE FOR RESIDUE AMP C 843 source : AC7 4) chain D residue 14 type sequence S description BINDING SITE FOR RESIDUE SO4 C 845 source : AC9 5) chain D residue 16 type sequence R description BINDING SITE FOR RESIDUE SO4 C 845 source : AC9 6) chain D residue 69 type sequence R description BINDING SITE FOR RESIDUE SO4 C 845 source : AC9 7) chain D residue 67 type sequence W description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 8) chain D residue 71 type sequence Q description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 9) chain D residue 75 type sequence Y description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 10) chain D residue 309 type sequence R description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 11) chain D residue 310 type sequence R description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 12) chain D residue 315 type sequence K description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 13) chain D residue 317 type sequence G description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 14) chain D residue 318 type sequence C description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 15) chain D residue 43 type sequence R description BINDING SITE FOR RESIDUE SO4 D 844 source : BC2 16) chain D residue 135 type sequence G description BINDING SITE FOR RESIDUE SO4 D 845 source : BC3 17) chain D residue 569 type sequence R description BINDING SITE FOR RESIDUE SO4 D 845 source : BC3 18) chain D residue 574 type sequence K description BINDING SITE FOR RESIDUE SO4 D 845 source : BC3 19) chain D residue 680 type sequence X description BINDING SITE FOR RESIDUE SO4 D 845 source : BC3 20) chain D residue 513 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 21) chain D residue 746 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 22) chain D residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 23) 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 24) chain D residue 42 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 25) chain D residue 309 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 26) chain D residue 75 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 27) 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 28) 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 29) 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 30) 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 31) chain D residue 203 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 32) chain D residue 226 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 33) chain D residue 429 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 34) chain D residue 472 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9 35) chain D residue 377 type catalytic sequence H description 205 source MCSA : MCSA4 36) chain D residue 568 type catalytic sequence K description 205 source MCSA : MCSA4 37) chain D residue 569 type catalytic sequence R description 205 source MCSA : MCSA4 38) chain D residue 574 type catalytic sequence K description 205 source MCSA : MCSA4 39) chain D residue 676 type catalytic sequence T description 205 source MCSA : MCSA4 40) chain D residue 680 type catalytic sequence X description 205 source MCSA : MCSA4

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