eF-site ID 1di9-A PDB Code 1di9 Chain A click to enlarge Title THE STRUCTURE OF P38 MITOGEN-ACTIVATED PROTEIN KINASE IN COMPLEX WITH 4-[3-METHYLSULFANYLANILINO]-6,7-DIMETHOXYQUINAZOLINE Classification TRANSFERASE Compound P38 KINASE Source null (MK14_HUMAN) Sequence A:  ERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFD TKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENV IGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLT DDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCE LKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQT VDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPG AELLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVD LLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVADPY DQSFESRDLLIDEWKSLTYDEVISFVPP Description Functional site 1) chain A residue 30 type sequence V description BINDING SITE FOR RESIDUE MSQ A 500 source : AC1 2) chain A residue 51 type sequence A description BINDING SITE FOR RESIDUE MSQ A 500 source : AC1 3) chain A residue 53 type sequence K description BINDING SITE FOR RESIDUE MSQ A 500 source : AC1 4) chain A residue 71 type sequence E description BINDING SITE FOR RESIDUE MSQ A 500 source : AC1 5) chain A residue 104 type sequence L description BINDING SITE FOR RESIDUE MSQ A 500 source : AC1 6) chain A residue 106 type sequence T description BINDING SITE FOR RESIDUE MSQ A 500 source : AC1 7) chain A residue 107 type sequence H description BINDING SITE FOR RESIDUE MSQ A 500 source : AC1 8) chain A residue 108 type sequence L description BINDING SITE FOR RESIDUE MSQ A 500 source : AC1 9) chain A residue 109 type sequence M description BINDING SITE FOR RESIDUE MSQ A 500 source : AC1 10) chain A residue 53 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:21444723 source Swiss-Prot : SWS_FT_FI5 11) chain A residue 152 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:21444723 source Swiss-Prot : SWS_FT_FI5 12) chain A residue 30-54 type prosite sequence VGSGAYGSVCAAFDTKTGLRVAVKK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGSGAYGSVCaAfdtktglrv.........AVKK source prosite : PS00107 13) chain A residue 59-162 type prosite sequence FQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEE FNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGL KYIHSADIIHRDLKPSNLAVNEDC description MAPK MAP kinase signature. FqsiihakrtyRElrllkhmkhenviglldvftparsleefndvylvthlmgadlnnivkcqkltddhvqfliyqilrglkyihsadiih.........RDlKpsnlavnedC source prosite : PS01351 14) chain A residue 16 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18691976 source Swiss-Prot : SWS_FT_FI4 15) chain A residue 263 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17525332 source Swiss-Prot : SWS_FT_FI8 16) chain A residue 180 type MOD_RES sequence T description Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysis => ECO:0000269|PubMed:7535770, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 17) chain A residue 182 type MOD_RES sequence Y description Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysis => ECO:0000269|PubMed:7535770, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 18) chain A residue 323 type MOD_RES sequence Y description Phosphotyrosine; by ZAP70 => ECO:0000269|PubMed:15735648 source Swiss-Prot : SWS_FT_FI9 19) chain A residue 168 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 20) chain A residue 53 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 21) chain A residue 30 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI2

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