eF-site ID 2gm9-A PDB Code 2gm9 Chain A click to enlarge Title Structure of rabbit muscle glycogen phosphorylase in complex with thienopyrrole Classification TRANSFERASE Compound Glycogen phosphorylase, muscle form Source ORGANISM_COMMON: rabbit; ORGANISM_SCIENTIFIC: Oryctolagus cuniculus; Sequence A:  QISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDY YFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYM GRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGL GNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIC GGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQ GAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNG GYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVV AATLQDIIRRFKSNFDAFPDKVAIQLNDTHPSLAIPELMR VLVDLERLDWDKAWEVTVKTCAYTNHTVLPEALERWPVHL LETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLV EEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDF YELEPHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEY ISDLDQLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLER EYKVHINPNSLFDVQVKRIHEYKRQLLNCLHVITLYNRIK KEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVVN HDPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGT EASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIF GMRVEDVDRLDQRGYNAQEYYDRIPELRQIIEQLSSGFFS PKQPDLFKDIVNMLMHHDRFKVFADYEEYVKCQERVSALY KNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSR QRLPA Description Functional site 1) chain A residue 90 type sequence Y description BINDING SITE FOR RESIDUE PLR A 900 source : AC1 2) chain A residue 134 type sequence G description BINDING SITE FOR RESIDUE PLR A 900 source : AC1 3) chain A residue 491 type sequence W description BINDING SITE FOR RESIDUE PLR A 900 source : AC1 4) chain A residue 567 type sequence V description BINDING SITE FOR RESIDUE PLR A 900 source : AC1 5) chain A residue 568 type sequence K description BINDING SITE FOR RESIDUE PLR A 900 source : AC1 6) chain A residue 574 type sequence K description BINDING SITE FOR RESIDUE PLR A 900 source : AC1 7) chain A residue 648 type sequence Y description BINDING SITE FOR RESIDUE PLR A 900 source : AC1 8) chain A residue 649 type sequence R description BINDING SITE FOR RESIDUE PLR A 900 source : AC1 9) chain A residue 650 type sequence V description BINDING SITE FOR RESIDUE PLR A 900 source : AC1 10) chain A residue 675 type sequence G description BINDING SITE FOR RESIDUE PLR A 900 source : AC1 11) chain A residue 676 type sequence T description BINDING SITE FOR RESIDUE PLR A 900 source : AC1 12) chain A residue 677 type sequence G description BINDING SITE FOR RESIDUE PLR A 900 source : AC1 13) chain A residue 680 type sequence K description BINDING SITE FOR RESIDUE PLR A 900 source : AC1 14) chain A residue 37 type sequence F description BINDING SITE FOR RESIDUE 3TH A 1 source : AC2 15) chain A residue 38 type sequence T description BINDING SITE FOR RESIDUE 3TH A 1 source : AC2 16) chain A residue 40 type sequence V description BINDING SITE FOR RESIDUE 3TH A 1 source : AC2 17) chain A residue 53 type sequence F description BINDING SITE FOR RESIDUE 3TH A 1 source : AC2 18) chain A residue 57 type sequence H description BINDING SITE FOR RESIDUE 3TH A 1 source : AC2 19) chain A residue 60 type sequence R description BINDING SITE FOR RESIDUE 3TH A 1 source : AC2 20) chain A residue 67 type sequence W description BINDING SITE FOR RESIDUE 3TH A 1 source : AC2 21) chain A residue 185 type sequence Y description BINDING SITE FOR RESIDUE 3TH A 1 source : AC2 22) chain A residue 188 type sequence P description BINDING SITE FOR RESIDUE 3TH A 1 source : AC2 23) chain A residue 189 type sequence W description BINDING SITE FOR RESIDUE 3TH A 1 source : AC2 24) chain A residue 190 type sequence E description BINDING SITE FOR RESIDUE 3TH A 1 source : AC2 25) chain A residue 191 type sequence K description BINDING SITE FOR RESIDUE 3TH A 1 source : AC2 26) chain A residue 514 type MOD_RES sequence D description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI9 27) chain A residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI9 28) chain A residue 748 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI9 29) chain A residue 681 type MOD_RES sequence F 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_FI10 30) chain A residue 43 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 310 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 76 type BINDING sequence E description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 33) chain A residue 109 type SITE sequence D description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 143 type SITE sequence F description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 35) chain A residue 156 type SITE sequence G description Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI4 36) chain A residue 15 type MOD_RES sequence V description Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI5 37) chain A residue 204 type MOD_RES sequence G description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI6 38) chain A residue 227 type MOD_RES sequence D description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI6 39) chain A residue 430 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI7 40) chain A residue 473 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 41) chain A residue 672-684 type prosite sequence EASGTGNMKFMLN description PHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKfmLN source prosite : PS00102 42) chain A residue 378 type catalytic sequence T description 205 source MCSA : MCSA1 43) chain A residue 569 type catalytic sequence R description 205 source MCSA : MCSA1 44) chain A residue 570 type catalytic sequence I description 205 source MCSA : MCSA1 45) chain A residue 575 type catalytic sequence R description 205 source MCSA : MCSA1 46) chain A residue 677 type catalytic sequence G description 205 source MCSA : MCSA1 47) chain A residue 681 type catalytic sequence F description 205 source MCSA : MCSA1

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