eF-site ID 3e3n-A PDB Code 3e3n Chain A 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 A:  QEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVA TPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLS LEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIE EDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIF NQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRV EHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSA KAPNGYIQAVLDRNLAENISRVLYGKELRLKQEYFVVAAT LQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPS LAIPELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVLPEA LERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVD RLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEIL KKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEII AERIGEEYISDLDQLRKLLSYVDDEAFIRDVAKVKQENKL KFAAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHV ITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLI TAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLS EQISTAGTEASGTGNMXFMLNGALTIGTMDGANVEMAEEA GEENFFIFGMRVEDVDRLDQRGYNAQEYYDRIPELRQIIE QLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVKC QERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYARE IWGVEPSRQRLPAP 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 A residue 14 type sequence S description BINDING SITE FOR RESIDUE SO4 A 844 source : AC2 11) chain A residue 16 type sequence R description BINDING SITE FOR RESIDUE SO4 A 844 source : AC2 12) chain A residue 69 type sequence R description BINDING SITE FOR RESIDUE SO4 A 844 source : AC2 13) chain A residue 135 type sequence G description BINDING SITE FOR RESIDUE SO4 A 845 source : AC3 14) chain A residue 569 type sequence R description BINDING SITE FOR RESIDUE SO4 A 845 source : AC3 15) chain A residue 574 type sequence K description BINDING SITE FOR RESIDUE SO4 A 845 source : AC3 16) chain A residue 42 type sequence D description BINDING SITE FOR RESIDUE AMP B 843 source : AC4 17) chain A residue 44 type sequence N description BINDING SITE FOR RESIDUE AMP B 843 source : AC4 18) chain A residue 45 type sequence V description BINDING SITE FOR RESIDUE AMP B 843 source : AC4 19) chain A residue 43 type sequence R description BINDING SITE FOR RESIDUE SO4 B 844 source : AC5 20) chain A residue 513 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 21) chain A residue 746 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 22) chain A residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 23) 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 24) chain A residue 42 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 309 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 75 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 27) 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 28) 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 29) 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 30) 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 31) chain A residue 203 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 32) chain A residue 226 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 33) chain A residue 429 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 34) chain A residue 472 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9 35) chain A residue 672-684 type prosite sequence EASGTGNMXFMLN description PHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKfmLN source prosite : PS00102 36) chain A residue 377 type catalytic sequence H description 205 source MCSA : MCSA1 37) chain A residue 568 type catalytic sequence K description 205 source MCSA : MCSA1 38) chain A residue 569 type catalytic sequence R description 205 source MCSA : MCSA1 39) chain A residue 574 type catalytic sequence K description 205 source MCSA : MCSA1 40) chain A residue 676 type catalytic sequence T description 205 source MCSA : MCSA1 41) chain A residue 680 type catalytic sequence X description 205 source MCSA : MCSA1

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