eF-site ID 4uy9-AB PDB Code 4uy9 Chain A, B click to enlarge Title Structure of MLK1 kinase domain with leucine zipper 1 Classification TRANSFERASE Compound MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 9 Source (M3K9_HUMAN) Sequence A:  QLLEIDFAELTLEEIIGIGGFGKVYRAFWIGDEVAVKAAR HDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEP NLCLVMEFARGGPLNRVLSGKRIPPDILVNWAVQIARGMN YLHDEAIVPIIHRDLKSSNILILQKVENGDLSNKILKITD FGLAREWHRTTKMSAAGTYAWMAPEVIRASMFSKGSDVWS YGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLALPIPSTC PEPFAKLMEDCWNPDPHSRPSFTNILDQLTTIEESGFFEM PKDSFHCLQDNWKHEIQEMFDQLRAKEKELRTW B:  QLLEIDFAELTLEEIIGIGGFGKVYRAFWIGDEVAVKAAR HDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEP NLCLVMEFARGGPLNRVLSGKRIPPDILVNWAVQIARGMN YLHDEAIVPIIHRDLKSSNILILQKVENGDLSNKILKITD FGLAREWHRTTKMSAAGTYAWMAPEVIRASMFSKGSDVWS YGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLALPIPSTC PEPFAKLMEDCWNPDPHSRPSFTNILDQLTTIEESGFFEM PKDSFHCLQDNWKHEIQEMFDQLRAKEKELRTWEE Description Functional site 1) chain A residue 150-171 type prosite sequence IGIGGFGKVYRAFWIGDEVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGIGGFGKVYrAfwigde............VAVK source prosite : PS00107 2) chain A residue 264-276 type prosite sequence IIHRDLKSSNILI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKssNILI source prosite : PS00108 3) chain A residue 308 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000269|PubMed:15610029 source Swiss-Prot : SWS_FT_FI5 4) chain B residue 308 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000269|PubMed:15610029 source Swiss-Prot : SWS_FT_FI5 5) chain A residue 268 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 6) chain B residue 268 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 7) chain A residue 150 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 8) chain B residue 150 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 9) chain A residue 171 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 10) chain B residue 171 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 11) chain A residue 304 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:15610029 source Swiss-Prot : SWS_FT_FI4 12) chain A residue 305 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:15610029 source Swiss-Prot : SWS_FT_FI4 13) chain A residue 312 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:15610029 source Swiss-Prot : SWS_FT_FI4 14) chain B residue 304 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:15610029 source Swiss-Prot : SWS_FT_FI4 15) chain B residue 305 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:15610029 source Swiss-Prot : SWS_FT_FI4 16) chain B residue 312 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:15610029 source Swiss-Prot : SWS_FT_FI4

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