eF-site ID 1cm8-AB PDB Code 1cm8 Chain A, B click to enlarge Title PHOSPHORYLATED MAP KINASE P38-GAMMA Classification TRANSFERASE Compound PHOSPHORYLATED MAP KINASE P38-GAMMA Source Homo sapiens (Human) (MK12_HUMAN) Sequence A:  RSGFYRQEVTKTAWEVRAVYRDLQPVAVCSAVDGRTGAKV AIKKLYRPFQSELFAKRAYRELRLLKHMRHENVIGLLDVF TPDETLDDFTDFYLVMPFMGTDLGKLMKHEKLGEDRIQFL VYQMLKGLRYIHAAGIIHRDLKPGNLAVNEDCELKILDFG LARQADSEMXGXVVTRWYRAPEVILNWMRYTQTVDIWSVG CIMAEMITGKTLFKGSDHLDQLKEIMKVTGTPPAEFVQRL QSDEAKNYMKGLPELEKKDFASILTNASPLAVNLLEKMLV LDAEQRVTAGEALAHPYFESLHQVQKYDDSRTLDEWKRVT YKEVLSFKP B:  RSGFYRQEVTKTAWEVRAVYRDLQPVAVCSAVDGRTGAKV AIKKLYRPFQSELFAKRAYRELRLLKHMRHENVIGLLDVF TPDETLDDFTDFYLVMPFMGTDLGKLMKHEKLGEDRIQFL VYQMLKGLRYIHAAGIIHRDLKPGNLAVNEDCELKILDFG LARQADSEMXGXVVTRWYRAPEVILNWMRYTQTVDIWSVG CIMAEMITGKTLFKGSDHLDQLKEIMKVTGTPPAEFVQRL QSDEAKNYMKGLPELEKKDFASILTNASPLAVNLLEKMLV LDAEQRVTAGEALAHPYFESLHQVQKYDDSRTLDEWKRVT YKEVLSFKP Description Functional site 1) chain A residue 158 type sequence N description BINDING SITE FOR RESIDUE MG A 401 source : AC1 2) chain A residue 171 type sequence D description BINDING SITE FOR RESIDUE MG A 401 source : AC1 3) chain A residue 171 type sequence D description BINDING SITE FOR RESIDUE MG A 402 source : AC2 4) chain B residue 1158 type sequence N description BINDING SITE FOR RESIDUE MG B 1401 source : AC3 5) chain B residue 1171 type sequence D description BINDING SITE FOR RESIDUE MG B 1401 source : AC3 6) chain B residue 1171 type sequence D description BINDING SITE FOR RESIDUE MG B 1402 source : AC4 7) chain A residue 41 type sequence V description BINDING SITE FOR RESIDUE ANP A 400 source : AC5 8) chain A residue 54 type sequence A description BINDING SITE FOR RESIDUE ANP A 400 source : AC5 9) chain A residue 56 type sequence K description BINDING SITE FOR RESIDUE ANP A 400 source : AC5 10) chain A residue 87 type sequence I description BINDING SITE FOR RESIDUE ANP A 400 source : AC5 11) chain A residue 109 type sequence M description BINDING SITE FOR RESIDUE ANP A 400 source : AC5 12) chain A residue 110 type sequence P description BINDING SITE FOR RESIDUE ANP A 400 source : AC5 13) chain A residue 112 type sequence M description BINDING SITE FOR RESIDUE ANP A 400 source : AC5 14) chain A residue 115 type sequence D description BINDING SITE FOR RESIDUE ANP A 400 source : AC5 15) chain A residue 155 type sequence K description BINDING SITE FOR RESIDUE ANP A 400 source : AC5 16) chain A residue 157 type sequence G description BINDING SITE FOR RESIDUE ANP A 400 source : AC5 17) chain A residue 158 type sequence N description BINDING SITE FOR RESIDUE ANP A 400 source : AC5 18) chain A residue 170 type sequence L description BINDING SITE FOR RESIDUE ANP A 400 source : AC5 19) chain A residue 171 type sequence D description BINDING SITE FOR RESIDUE ANP A 400 source : AC5 20) chain B residue 1041 type sequence V description BINDING SITE FOR RESIDUE ANP B 1400 source : AC6 21) chain B residue 1054 type sequence A description BINDING SITE FOR RESIDUE ANP B 1400 source : AC6 22) chain B residue 1056 type sequence K description BINDING SITE FOR RESIDUE ANP B 1400 source : AC6 23) chain B residue 1087 type sequence I description BINDING SITE FOR RESIDUE ANP B 1400 source : AC6 24) chain B residue 1109 type sequence M description BINDING SITE FOR RESIDUE ANP B 1400 source : AC6 25) chain B residue 1110 type sequence P description BINDING SITE FOR RESIDUE ANP B 1400 source : AC6 26) chain B residue 1112 type sequence M description BINDING SITE FOR RESIDUE ANP B 1400 source : AC6 27) chain B residue 1115 type sequence D description BINDING SITE FOR RESIDUE ANP B 1400 source : AC6 28) chain B residue 1155 type sequence K description BINDING SITE FOR RESIDUE ANP B 1400 source : AC6 29) chain B residue 1157 type sequence G description BINDING SITE FOR RESIDUE ANP B 1400 source : AC6 30) chain B residue 1158 type sequence N description BINDING SITE FOR RESIDUE ANP B 1400 source : AC6 31) chain B residue 1170 type sequence L description BINDING SITE FOR RESIDUE ANP B 1400 source : AC6 32) chain B residue 1171 type sequence D description BINDING SITE FOR RESIDUE ANP B 1400 source : AC6 33) chain A residue 153 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 1153 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 33 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 36) chain A residue 56 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 37) chain B residue 1033 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 38) chain B residue 1056 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 183 type MOD_RES sequence X description Phosphothreonine; by MAP2K3 and MAP2K6 => ECO:0000250|UniProtKB:Q63538 source Swiss-Prot : SWS_FT_FI3 40) chain B residue 1183 type MOD_RES sequence X description Phosphothreonine; by MAP2K3 and MAP2K6 => ECO:0000250|UniProtKB:Q63538 source Swiss-Prot : SWS_FT_FI3 41) chain A residue 185 type MOD_RES sequence X description Phosphotyrosine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 42) chain B residue 1185 type MOD_RES sequence X description Phosphotyrosine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 43) chain A residue 33-57 type prosite sequence VAVCSAVDGRTGAKVAIKK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGSGAYGAVCsAvdgrtgakv.........AIKK source prosite : PS00107 44) chain A residue 62-165 type prosite sequence FQSELFAKRAYRELRLLKHMRHENVIGLLDVFTPDETLDD FTDFYLVMPFMGTDLGKLMKHEKLGEDRIQFLVYQMLKGL RYIHAAGIIHRDLKPGNLAVNEDC description MAPK MAP kinase signature. FqselfakrayRElrllkhmrhenviglldvftpdetlddftdfylvmpfmgtdlgklmkheklgedriqflvyqmlkglryihaagiih.........RDlKpgnlavnedC source prosite : PS01351

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