eF-site ID 3e3n-E PDB Code 3e3n Chain E 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 E:  EKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVAT PRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSL EFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEE DAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFN QKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVE HTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAK APNGYIQAVLDRNLAENISRVLYGKELRLKQEYFVVAATL QDIIRRFKSSNFDAFPDKVAIQLNDTHPSLAIPELMRVLV DLERLDWDKAWEVTVKTCAYTNHTVLPEALERWPVHLLET LLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEG AVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYEL EPHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISD LDQLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLEREYK VHINPNSLFDVQVKRIHEYKRQLLNCLHVITLYNRIKKEP NKFVVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVVNHDP VVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEAS GTGNMXFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMR VEDVDRLDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQ PDLFKDIVNMLMHHDRFKVFADYEEYVKCQERVSALYKNP REWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRL PAP Description Functional site 1) chain E residue 67 type sequence W description BINDING SITE FOR RESIDUE AMP E 843 source : BC4 2) chain E residue 71 type sequence Q description BINDING SITE FOR RESIDUE AMP E 843 source : BC4 3) chain E residue 75 type sequence Y description BINDING SITE FOR RESIDUE AMP E 843 source : BC4 4) chain E residue 309 type sequence R description BINDING SITE FOR RESIDUE AMP E 843 source : BC4 5) chain E residue 310 type sequence R description BINDING SITE FOR RESIDUE AMP E 843 source : BC4 6) chain E residue 14 type sequence S description BINDING SITE FOR RESIDUE SO4 E 844 source : BC5 7) chain E residue 16 type sequence R description BINDING SITE FOR RESIDUE SO4 E 844 source : BC5 8) chain E residue 69 type sequence R description BINDING SITE FOR RESIDUE SO4 E 844 source : BC5 9) chain E residue 135 type sequence G description BINDING SITE FOR RESIDUE SO4 E 845 source : BC6 10) chain E residue 569 type sequence R description BINDING SITE FOR RESIDUE SO4 E 845 source : BC6 11) chain E residue 680 type sequence X description BINDING SITE FOR RESIDUE SO4 E 845 source : BC6 12) chain E residue 42 type sequence D description BINDING SITE FOR RESIDUE AMP F 843 source : BC7 13) chain E residue 44 type sequence N description BINDING SITE FOR RESIDUE AMP F 843 source : BC7 14) chain E residue 45 type sequence V description BINDING SITE FOR RESIDUE AMP F 843 source : BC7 15) chain E residue 43 type sequence R description BINDING SITE FOR RESIDUE SO4 F 844 source : BC8 16) chain E residue 377 type catalytic sequence H description 205 source MCSA : MCSA5 17) chain E residue 568 type catalytic sequence K description 205 source MCSA : MCSA5 18) chain E residue 569 type catalytic sequence R description 205 source MCSA : MCSA5 19) chain E residue 574 type catalytic sequence K description 205 source MCSA : MCSA5 20) chain E residue 676 type catalytic sequence T description 205 source MCSA : MCSA5 21) chain E residue 680 type catalytic sequence X description 205 source MCSA : MCSA5 22) chain E 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 23) chain E residue 309 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 24) chain E residue 42 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P11217 source Swiss-Prot : SWS_FT_FI1 25) chain E residue 75 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:3616621 source Swiss-Prot : SWS_FT_FI2 26) chain E residue 142 type SITE sequence C description Involved in the association of subunits => ECO:0000303|PubMed:728424 source Swiss-Prot : SWS_FT_FI3 27) chain E 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 E residue 513 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 29) chain E residue 746 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 30) chain E residue 747 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI10 31) chain E 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 32) chain E 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 33) chain E residue 226 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 34) chain E residue 203 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P09812 source Swiss-Prot : SWS_FT_FI7 35) chain E residue 429 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI8 36) chain E residue 472 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 source Swiss-Prot : SWS_FT_FI9

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