eF-site ID 3e3n-C PDB Code 3e3n Chain C 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 C:  KRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATP RDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLE FYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEED AGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQ KICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEH TSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKA PNGYIQAVLDRNLAENISRVLYGKELRLKQEYFVVAATLQ DIIRRFKSSNFDAFPDKVAIQLNDTHPSLAIPELMRVLVD LERLDWDKAWEVTVKTCAYTNHTVLPEALERWPVHLLETL LPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGA VKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELE PHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISDL DQLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLEREYKV HINPNSLFDVQVKRIHEYKRQLLNCLHVITLYNRIKKEPN KFVVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVVNHDPV VGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASG TGNMXFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRV EDVDRLDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQP DLFKDIVNMLMHHDRFKVFADYEEYVKCQERVSALYKNPR EWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLP AP Description Functional site 1) chain C residue 67 type sequence W description BINDING SITE FOR RESIDUE AMP C 843 source : AC7 2) chain C residue 71 type sequence Q description BINDING SITE FOR RESIDUE AMP C 843 source : AC7 3) chain C residue 75 type sequence Y description BINDING SITE FOR RESIDUE AMP C 843 source : AC7 4) chain C residue 309 type sequence R description BINDING SITE FOR RESIDUE AMP C 843 source : AC7 5) chain C residue 310 type sequence R description BINDING SITE FOR RESIDUE AMP C 843 source : AC7 6) chain C residue 135 type sequence G description BINDING SITE FOR RESIDUE SO4 C 844 source : AC8 7) chain C residue 569 type sequence R description BINDING SITE FOR RESIDUE SO4 C 844 source : AC8 8) chain C residue 574 type sequence K description BINDING SITE FOR RESIDUE SO4 C 844 source : AC8 9) chain C residue 680 type sequence X description BINDING SITE FOR RESIDUE SO4 C 844 source : AC8 10) chain C residue 43 type sequence R description BINDING SITE FOR RESIDUE SO4 C 845 source : AC9 11) chain C residue 42 type sequence D description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 12) chain C residue 44 type sequence N description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 13) chain C residue 45 type sequence V description BINDING SITE FOR RESIDUE AMP D 843 source : BC1 14) chain C residue 14 type sequence S description BINDING SITE FOR RESIDUE SO4 D 844 source : BC2 15) chain C residue 16 type sequence R description BINDING SITE FOR RESIDUE SO4 D 844 source : BC2 16) chain C residue 69 type sequence R description BINDING SITE FOR RESIDUE SO4 D 844 source : BC2 17) chain C residue 377 type catalytic sequence H description 205 source MCSA : MCSA3 18) chain C residue 568 type catalytic sequence K description 205 source MCSA : MCSA3 19) chain C residue 569 type catalytic sequence R description 205 source MCSA : MCSA3 20) chain C residue 574 type catalytic sequence K description 205 source MCSA : MCSA3 21) chain C residue 676 type catalytic sequence T description 205 source MCSA : MCSA3 22) chain C residue 680 type catalytic sequence X description 205 source MCSA : MCSA3 23) chain C 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 24) chain C residue 42 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 25) chain C residue 309 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 26) chain C residue 75 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 27) chain C 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 C 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 C residue 513 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 30) chain C residue 746 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 31) chain C residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 32) chain C 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 33) chain C 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 34) chain C residue 203 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 35) chain C residue 226 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 36) chain C residue 429 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 37) chain C residue 472 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9

Display surface Download Links