eF-site ID 2ojg-A PDB Code 2ojg Chain A click to enlarge Title Crystal structure of ERK2 in complex with N,N-dimethyl-4-(4-phenyl-1H-pyrazol-3-yl)-1H-pyrrole-2-carboxamide Classification TRANSFERASE Compound Mitogen-activated protein kinase 1 Source Homo sapiens (Human) (MK01_HUMAN) Sequence A:  FDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISP FEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQM KDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLK YIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDH DHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCIL AEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINL KARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNP HKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFELDDLPK EKLKELIFEETARFQPG Description Functional site 1) chain A residue 189 type sequence R description BINDING SITE FOR RESIDUE SO4 A 359 source : AC1 2) chain A residue 192 type sequence R description BINDING SITE FOR RESIDUE SO4 A 359 source : AC1 3) chain A residue 231 type sequence Y description BINDING SITE FOR RESIDUE SO4 A 359 source : AC1 4) chain A residue 29 type sequence I description BINDING SITE FOR RESIDUE 19A A 360 source : AC2 5) chain A residue 34 type sequence Y description BINDING SITE FOR RESIDUE 19A A 360 source : AC2 6) chain A residue 37 type sequence V description BINDING SITE FOR RESIDUE 19A A 360 source : AC2 7) chain A residue 50 type sequence A description BINDING SITE FOR RESIDUE 19A A 360 source : AC2 8) chain A residue 52 type sequence K description BINDING SITE FOR RESIDUE 19A A 360 source : AC2 9) chain A residue 82 type sequence I description BINDING SITE FOR RESIDUE 19A A 360 source : AC2 10) chain A residue 103 type sequence Q description BINDING SITE FOR RESIDUE 19A A 360 source : AC2 11) chain A residue 104 type sequence D description BINDING SITE FOR RESIDUE 19A A 360 source : AC2 12) chain A residue 105 type sequence L description BINDING SITE FOR RESIDUE 19A A 360 source : AC2 13) chain A residue 106 type sequence M description BINDING SITE FOR RESIDUE 19A A 360 source : AC2 14) chain A residue 109 type sequence D description BINDING SITE FOR RESIDUE 19A A 360 source : AC2 15) chain A residue 112 type sequence K description BINDING SITE FOR RESIDUE 19A A 360 source : AC2 16) chain A residue 154 type sequence L description BINDING SITE FOR RESIDUE 19A A 360 source : AC2 17) chain A residue 165 type sequence D description BINDING SITE FOR RESIDUE 19A A 360 source : AC2 18) chain A residue 258-276 type DNA_BIND sequence ARNYLLSLPHKNKVPWNRL description source Swiss-Prot : SWS_FT_FI1 19) chain A residue 30 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 53 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 29-53 type prosite sequence IGEGAYGMVCSAYDNVNKVRVAIKK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGAYGMVCsAydnvnkvrv.........AIKK source prosite : PS00107 22) chain A residue 143-155 type prosite sequence VLHRDLKPSNLLL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpsNLLL source prosite : PS00108 23) chain A residue 57-159 type prosite sequence FEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQM KDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLK YIHSANVLHRDLKPSNLLLNTTC description MAPK MAP kinase signature. FehqtycqrtlREikillrfrheniigindiiraptieqmkdvyivqdlmetdlykllktqhlsndhicyflyqilrglkyihsanvlh..........RDlKpsnlllnttC source prosite : PS01351 24) chain A residue 283 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI10 25) chain A residue 28 type MOD_RES sequence Y description Phosphoserine; by SGK1 => ECO:0000269|PubMed:19447520 source Swiss-Prot : SWS_FT_FI5 26) chain A residue 184 type MOD_RES sequence E description Phosphothreonine; by MAP2K1 and MAP2K2 => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 27) chain A residue 148 type ACT_SITE sequence L description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 186 type MOD_RES sequence V description Phosphotyrosine; by MAP2K1 and MAP2K2 => ECO:0000269|PubMed:19053285, ECO:0000269|PubMed:19494114, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 29) chain A residue 189 type MOD_RES sequence R description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:19060905 source Swiss-Prot : SWS_FT_FI8 30) chain A residue 245 type MOD_RES sequence P description Phosphoserine => ECO:0000269|PubMed:18760948 source Swiss-Prot : SWS_FT_FI9 31) chain A residue 247 type MOD_RES sequence Q description Phosphoserine => ECO:0000269|PubMed:18760948 source Swiss-Prot : SWS_FT_FI9

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