eF-site ID 6yve-.AAA PDB Code 6yve Chain AAA click to enlarge Title Glycogen phosphorylase b in complex with pelargonidin 3-O-beta-D-glucoside Classification TRANSFERASE Compound Glycogen phosphorylase, muscle form Source ORGANISM_COMMON: Rabbit; ORGANISM_SCIENTIFIC: Oryctolagus cuniculus; Sequence AAA:  QISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDY YFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYM GRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGL GNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIC GGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQ GAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPND FVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEY FVVAATLQDIIRRFKSSKFNFDAFPDKVAIQLNDTHPSLA IPELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVLPEALE RWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRL RRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKK TIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEIIAE RIGEEYISDLDQLRKLLSYVDDEAFIRDVAKVKQENKLKF AAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHVIT LYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITA IGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQ ISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGE ENFFIFGMRVEDVDRLDQRGYNAQEYYDRIPELRQIIEQL SSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVKCQE RVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIW GVEPSRQRLPA Description Functional site 1) chain AAA residue 377 type catalytic sequence H description 205 source MCSA : MCSA1 2) chain AAA residue 568 type catalytic sequence K description 205 source MCSA : MCSA1 3) chain AAA residue 569 type catalytic sequence R description 205 source MCSA : MCSA1 4) chain AAA residue 574 type catalytic sequence K description 205 source MCSA : MCSA1 5) chain AAA residue 676 type catalytic sequence T description 205 source MCSA : MCSA1 6) chain AAA residue 680 type catalytic sequence K description 205 source MCSA : MCSA1 7) chain AAA residue 42 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 8) chain AAA residue 309 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 9) chain AAA residue 75 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 10) chain AAA residue 108 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 11) chain AAA residue 142 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 12) chain AAA 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 13) chain AAA 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 14) chain AAA residue 203 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 15) chain AAA residue 226 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 16) chain AAA residue 429 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 17) chain AAA residue 472 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9 18) chain AAA residue 513 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 19) chain AAA residue 746 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 20) chain AAA residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 21) chain AAA residue 680 type MOD_RES sequence K 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 22) chain AAA residue 672-684 type prosite sequence EASGTGNMKFMLN description PHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKfmLN source prosite : PS00102

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